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Information on EC 2.1.2.1 - glycine hydroxymethyltransferase
for references in articles please use BRENDA:EC2.1.2.1
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.2 Hydroxymethyl-, formyl- and related transferases
2.1.2.1 glycine hydroxymethyltransferase
IUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 2.1.2.1
-
one-carbon
- pyridoxal
- thymidylate
- purine
- 5'-phosphate
- homocysteine
- dihydrofolate
-
folate-dependent
-
photorespiratory
-
photorespiration
-
folate-mediated
- pyridoxal-5'-phosphate
- thf
- dtmp
- mthfd1
-
plp-dependent
-
remethylation
-
aldimine
- phgdh
- medicine
-
folate-metabolizing
- 5,10-methenyltetrahydrofolate
-
5'-phosphate-dependent
- antifolate
- hydroxypyruvate
-
quinonoid
- 5-methyltetrahydrofolate
- glycerate
- 5-formyltetrahydrofolate
- drug development
-
folate-related
- d-alanine
-
c1-tetrahydrofolate
-
1-carbon
-
5-formyl
- polyglutamate
- l-threonine
-
alpha-protons
-
slc19a1
-
retro-aldol
- degradation
- analysis
- synthesis
- biotechnology
- pharmacology
showSynonyms
serine hydroxymethyltransferase, shmt2, shmt1, serine hydroxymethyl transferase, serine transhydroxymethylase, serine hydroxymethyltransferase 2, mitochondrial serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, bsshmt, pvshmt, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AdSHMT
B5T_00815
bsSHMT
CgSHMT
EC 4.1.2.6
-
-
formerly
-
EcSHMT
eSHMT
GlyA
GlyA protein
glycine hydroxymethyltransferrase
GLYMA_08G108900
ITB serine hydroxylmethyltransferase
ITBSHMT_1
L-serine hydroxymethyltransferase
mesophilic SHMT
MJ1597
MSHMT
pSHMT
psychrophilic SHMT
serine hydroxymethyl transferase
serine hydroxymethylase hydroxymethyltransferase, serine
-
-
-
-
serine hydroxymethyltransferase
serine hydroxymethyltransferase 1
serine hydroxymethyltransferase 1, mitochondrial
serine hydroxymethyltransferase 2
serine hydroxymethyltransferase 8
serine hydroxymethyltransferase, cytosolic
serine hydroxymethyltransferase, mitochondrial
serine hydroxymethyltransferase-2
serine transhydroxymethylase
-
-
-
-
serine:H4F hydroxymethyltransferase
serine:tetrahydrofolate hydroxymethyltransferase
SHM1
SHM2
SHMT
SHMT-1
SHMT-L
SHMT-S
SHMT1
SHMT2
SHMT2alpha
SHMT8
Ta1509
Ta1509 protein
additional information
L-serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethyltransferase
-
-
-
-
serine hydroxymethyltransferase
-
serine hydroxymethyltransferase
-
serine hydroxymethyltransferase
-
-
serine hydroxymethyltransferase
-
serine hydroxymethyltransferase
Lathyrus oleraceus Progress 9
-
-
-
serine hydroxymethyltransferase
-
-
serine hydroxymethyltransferase
-
serine hydroxymethyltransferase, mitochondrial
SwissProt
SHMT
Lathyrus oleraceus Progress 9
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
enzyme exhibits threonine aldolase activity (EC 4.1.2.5), but the two enzymes are distinct
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
evidence for a direct transfer mechanism for the enzyme catalysed reaction
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
stereochemistry
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
general mechanism of pyridoxal 5'-phosphate-catalyzed aldolic cleavage, racemisation, and transamination reactions, and catalytic mechanism of the transaldimination reaction involving Tyr55, His228, and Arg235, overview. Tyr55 is contributed by the symmetry-related monomer, with respect to the pyridoxal 5'-phosphate-binding subunit, and functions as the general acid-base catalyst in this proton transfer
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5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
general mechanism of pyridoxal 5'-phosphate-catalyzed aldolic cleavage, racemisation, and transamination reactions, and catalytic mechanism of the transaldimination reaction involving Tyr55, His228, and Arg235, overview. Tyr55 is contributed by the symmetry-related monomer, with respect to the pyridoxal 5'-phosphate-binding subunit, and functions as the general acid-base catalyst in this proton transfer
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5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
the process of transimination involving serine and PLP at the active site of the SHMT enzyme takes place through different elementary steps such as the formation of the first geminal diamine intermediate (GDI1), transfer of a proton from the substrate serine to the phenolic oxygen of PLP, followed by another proton transfer from PLP to the amine nitrogen of lysine with the formation of the second geminal diamine intermediate (GDI2), and finally, detachment of the active site lysine residue from PLP to produce the external aldimine, reaction mechanism, overview
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
mechanism
-
-
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
dTMP de novo biosynthesis (mitochondrial), folate polyglutamylation, folate transformations I, folate transformations II (plants), folate transformations III (E. coli), formaldehyde assimilation I (serine pathway), glycine betaine degradation I, glycine betaine degradation II (mammalian), glycine betaine degradation III, glycine biosynthesis I, photorespiration I, photorespiration II, photorespiration III, purine nucleobases degradation II (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
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CAS REGISTRY NUMBER
COMMENTARY
9029-83-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
-
Substrates: the enzyme is a major source of one-carbon units for cellular metabolism. Potential for disruption of SHMT-mediated one-carbon metabolism by inadequate vitamin B-6 intake
Products: -
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r
5,6,7,8-tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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r
D-alanine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-3-hydroxy-L-isovaline + (3S)-4-(benzyloxy)-3-hydroxy-L-isovaline
Substrates: -
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?
D-alanine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-methylpropanoic acid
Substrates: -
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?
D-alanine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-methyl-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-methyl-5-phenyl-L-norvaline
Substrates: -
Products: -
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?
D-alanine + 4-(benzyloxy)butanal + H2O
(3R)-3-hydroxy-4-(3-phenylpropoxy)-L-isovaline + (3S)-3-hydroxy-4-(3-phenylpropoxy)-L-isovaline
Substrates: -
Products: -
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?
D-alanine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-methylpropanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-methylpropanoic acid
Substrates: -
Products: -
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?
D-alanine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-methylpropanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-methylpropanoic acid
Substrates: -
Products: -
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?
D-alanine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)-2-methylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)-2-methylpropanoic acid
Substrates: -
Products: -
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?
D-alanine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid
Substrates: -
Products: -
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?
D-alanine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid
Substrates: -
Products: -
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?
D-alanine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-L-isovaline
Substrates: -
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?
D-alanine + benzyl (3-oxopropyl)carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine + (2S,3R)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-methylhexanoic acid
Substrates: -
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?
D-alanine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-methyl-L-lysine
Substrates: -
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?
D-alanine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(3S,4S)-4-([(benzyloxy)carbonyl]amino)-3-hydroxy-2-methyl-L-norvaline + (3R,4S)-4-([(benzyloxy)carbonyl]amino)-3-hydroxy-2-methyl-L-norvaline
Substrates: -
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?
D-alanine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-methyl-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-(pentafluorophenyl)propanoic acid
Substrates: -
Products: -
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?
D-alanine + phenoxyacetaldehyde + H2O
(3R)-3-hydroxy-4-phenoxy-L-isovaline + (3S)-3-hydroxy-4-phenoxy-L-isovaline
Substrates: -
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?
D-alanine + phenylacetaldehyde + H2O
(3S)-3-hydroxy-4-phenyl-L-isovaline + (3R)-3-hydroxy-4-phenyl-L-isovaline
Substrates: -
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?
D-serine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline
D-serine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid
Substrates: -
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?
D-serine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline
Substrates: -
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?
D-serine + 4-(benzyloxy)butanal + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline
D-serine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid
Substrates: -
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?
D-serine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid
Substrates: -
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?
D-serine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid
Substrates: -
Products: -
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?
D-serine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid
Substrates: -
Products: -
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?
D-serine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid
Substrates: -
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?
D-serine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline
D-serine + benzyl (3-oxopropyl)carbamate + H2O
(3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine
Substrates: -
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?
D-serine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(3S,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline
Substrates: -
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?
D-serine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(3S,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline
Substrates: -
Products: -
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?
D-serine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid
Substrates: -
Products: -
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?
D-serine + phenoxyacetaldehyde + H2O
(3R)-2',3-dihydroxy-4-phenoxy-L-isovaline + (3S)-2',3-dihydroxy-4-phenoxy-L-isovaline
Substrates: -
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?
D-serine + phenylacetaldehyde + H2O
(3S)-2',3-dihydroxy-4-phenyl-L-isovaline + (3R)-2',3-dihydroxy-4-phenyl-L-isovaline
Substrates: -
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?
DL-3-phenylserine + ?
benzaldehyde + ?
Substrates: -
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?
glycine + (benzyloxy)acetaldehyde + H2O
(2S,3R)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid + (2S,3S)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
Substrates: -
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?
glycine + 2-fluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxypropanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxypropanoic acid
Substrates: -
Products: -
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?
glycine + 3-phenylpropanal + H2O
(3S)-3-hydroxy-5-phenyl-L-norvaline + (3R)-3-hydroxy-5-phenyl-L-norvaline
Substrates: -
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?
glycine + 4-(benzyloxy)butanal + H2O
(2S,3R)-2-amino-3-hydroxy-4-(3-phenylpropoxy)butanoic acid + (2S,3S)-2-amino-3-hydroxy-4-(3-phenylpropoxy)butanoic acid
Substrates: -
Products: -
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?
glycine + 4-chlorobenzaldehyde + H2O
(2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxypropanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxypropanoic acid
Substrates: -
Products: -
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?
glycine + 4-formylphenyl acetate + H2O
(2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxypropanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxypropanoic acid
Substrates: -
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?
glycine + 4-hydroxybenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-hydroxyphenyl)propanoic acid
Substrates: -
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?
glycine + 4-nitrobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
Substrates: -
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?
glycine + benzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-3-phenylpropanoic acid
Substrates: -
Products: -
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?
glycine + benzyl (2-oxoethyl)carbamate + H2O
(2S,3S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxybutanoic acid + (2S,3R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxybutanoic acid
Substrates: -
Products: -
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?
glycine + benzyl (3-oxopropyl)carbamate + H2O
(2S,3S)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxyhexanoic acid + (2S,3R)-2-amino-6-[[(benzyloxy)carbonyl]amino]-3-hydroxyhexanoic acid
Substrates: -
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?
glycine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O
(2S,3S,4R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-methylpentanoic acid + (2S,3S,4R)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid
Substrates: -
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?
glycine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O
(2S,3R,4S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid + (2S,3S,4S)-2-amino-4-[[(benzyloxy)carbonyl]amino]-3-hydroxypentanoic acid
Substrates: -
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?
glycine + pentafluorobenzaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(pentafluorophenyl)propanoic acid
Substrates: -
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?
glycine + phenoxyacetaldehyde + H2O
(2S,3R)-2-amino-3-hydroxy-4-phenoxybutanoic acid + (2S,3S)-2-amino-3-hydroxy-4-phenoxybutanoic acid
Substrates: -
Products: -
Products: -
?
glycine + phenylacetaldehyde + H2O
(2S,3S)-2-amino-3-hydroxy-4-phenylbutanoic acid + (2S,3R)-2-amino-3-hydroxy-4-phenylbutanoic acid
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
tetrahydromethanopterin + L-Ser
glycine + ?
-
Substrates: -
Products: -
Products: -
?
tetrahydropteroylglutamate + L-Ser
glycine + ?
-
Substrates: -
Products: -
Products: -
?
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: poor activity
Products: -
Products: -
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower
Products: -
Products: -
?
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: the enzyme also catalyzes the formation of methylene-tetrahydromethanopterin from tetrahydromethanopterin and L-serine, albeit with a catalytic efficiency which is less than 1% of that with (6S)-tetrahydrofolate as substrate. The catalytic efficiency with methylene-tetrahydrosarcinapterin as substrate is even lower
Products: -
Products: -
?
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methenyl-tetrahydropteroyl pentaglutamate + glycine + H2O
5-formyl-tetrahydropteroyl pentaglutamate + L-serine
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Aedes aegypti NIH Rockefeller
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: i.e. tetrahydropteroylglutamate, tetrahydropteroylglutamates with more than one glutamate residue are poor substrates and competitive inhibitors, overview
Products: i.e. tetrahydropteroylglutamate, tetrahydropteroylglutamates with more than one glutamate residue are poor substrates and competitive inhibitors, overview
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
A0A069BAT4
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
A0A069BAT4
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Lathyrus oleraceus Progress 9
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: tetrahydrofolate-dependent SHMT activity, modeling of substrate binding, overview
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: at high concentrations of enzyme
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
alpha-methylserine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
D-serine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + (benzyloxy)acetaldehyde + H2O
(3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + 4-(benzyloxy)butanal + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + 4-(benzyloxy)butanal + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + benzyl (2-oxoethyl)carbamate + H2O
(3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline
Substrates: -
Products: -
Products: -
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: the catalytic efficiency for D-serine is 580fold lower than that of L-serine
Products: -
Products: -
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: the catalytic efficiency for D-serine is 580fold lower than that of L-serine
Products: -
Products: -
?
D-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: the binding affinity for D-serine is 150fold lower than that of L-serine
Products: -
Products: -
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: placental conversion of serine to glycine is a major source of fetal glycine
Products: -
Products: -
?
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-Ser + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + modified folate
glycine + modified methylenefolate
Substrates: not: tetrahydrofolate, synthetic modified folate derivate
Products: -
Products: -
?
L-serine + modified folate
glycine + modified methylenefolate
Substrates: not: tetrahydrofolate, synthetic modified folate derivate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Q2TL58
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Q2TL58
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r, ?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: adding 2fold more glycine in the medium increases significantly the expression of SHMT-S and to an even higher level, the expression of SHMT-L, adding 2fold more serine has the reverse effect on the expression of SHMT-L, while the expression of SHMT-S does not change significantly
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: regulatory protein
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme is a component of thymidylate cycle
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme is a component of thymidylate cycle
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: only (6S)-tetrahydrofolate can serve as a substrate for His6-tagged SHMT, the presence of (6R)-tetrahydrofolate has no interference to the reaction
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: only (6S)-tetrahydrofolate can serve as a substrate for His6-tagged SHMT, the presence of (6R)-tetrahydrofolate has no interference to the reaction
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: L-serine is the physiological substrate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: SHMT antisense plants display lower photosynthetic capacity and accumulate glycine in light, glycine is converted to serine in the second half of the light period, serine shows an inverse diurnal rhythm and reaches highest values in darkness, glycine/serine conversion is independent of light in the transformant, but not in the wild-type
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: regulatory protein
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
Substrates: -
Products: -
Products: -
r
NADH + coenzyme Q10
?
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-Ser
5,10-methylenetetrahydrofolate + glycine
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Aedes aegypti NIH Rockefeller
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei CGMCC 1.3690
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei DSM 16502
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei MCCC 1A00001
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum CCUG 27702
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum NBRC 12168
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum NRRL B-2784
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Glycine max F650
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Mus musculus B6EiC3SnF1/J
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: L-serine is the best substrate
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychrobacter sp. ANT206
A0A7L7SZS9
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychromonas ingrahamii CCUG 51855
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychromonas ingrahamii DSM 17664
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Psychromonas ingrahamii CCUG 51855
Substrates: -
Products: -
Products: -
r
tetrahydropteroylglutamate + L-serine
5,10-methenyl-tetrahydropteroylglutamate + glycine + H2O
Psychromonas ingrahamii DSM 17664
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: the enzyme is also active with DL-threo-3-phenylserine
Products: -
Products: -
?
additional information
?
-
Substrates: purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified recombinant ApSHMT protein exhibits catalytic reactions for DL-threo-3-phenylserine as well as for L-serine
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is also active as threonine aldolase, EC 4.1.2.48
Products: -
Products: -
-
additional information
?
-
-
Substrates: SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate and reaction specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
Products: -
Products: -
?
additional information
?
-
-
Substrates: disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme catalyses the racemization of D- and L-alanine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyses the racemization of D- and L-alanine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 3-phenylserine is used as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate and reaction specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48
Products: -
Products: -
?
additional information
?
-
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme is also active as threonine aldolase, EC 4.1.2.48
Products: -
Products: -
-
additional information
?
-
-
Substrates: SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48
Products: -
Products: -
?
additional information
?
-
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
-
Substrates: no: D-allothreonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: D-allothreonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyses the racemization of D- and L-alanine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyses the racemization of D- and L-alanine
Products: -
Products: -
?
additional information
?
-
Substrates: SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme activity assay using a 5,10-methylenetetrahydrofolate dehydrogenase (MTHFD)-coupled reaction method. The enzyme is also active as threonine aldolase, EC 4.1.2.48. Analysis of enzyme binding structures of PLP-Gly and FTHF, overview. enzyme SHMT8 from Glycine max cv. Forrest has a severely impaired binding affinity for folate and 5-formyl-tetrahydrofolate (FTHF) and a corresponding defect in its folate-dependent enzyme activity
Products: -
Products: -
-
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an indispensable role in nucleic acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
Products: -
Products: -
?
additional information
?
-
-
Substrates: human serine hydroxymethyltransferase 2 binds specifically to heterogeneous nuclear ribonucleoprotein D
Products: -
Products: -
?
additional information
?
-
Substrates: DL-beta-phenylserine is used as substrate in activity assays, cf. EC 4.1.2.48
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
Products: -
Products: -
?
additional information
?
-
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: D-serine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: D-threonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: insoluble enzyme/antibody-complex shows 90% of original activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also catalyzes the tetrahydrofolate-independent retroaldol cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM1 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: SHM2 does not undergo half-transamination reaction with D-Ala resulting in the formation of the apoenzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits tetrahydrofolate-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: mutant enzyme H230Y catalyses oxidation of NADH, not wild type enzyme, H230A, H230F, H230N
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyses the racemization of D- and L-alanine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits THF-independent aldolase activity, EC 4.1.2.5, toward beta-hydroxyamino acids, producing glycine and aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: Plasmodium SHMT can use D-serine and L-serine as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyzes the tetrahydrofolate-independent retro-aldol cleavage of 3-hydroxy amino acids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: Plasmodium SHMT can use D-serine and L-serine as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: serine hydroxymethyltransferase is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes a hydroxymethyl group transfer from L-serine to tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
additional information
?
-
Substrates: L- and D-serine substrate binding structure analysis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: L- and D-serine substrate binding structure analysis, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also can synthesize L-threoning from glycine and acetaldehyde as well as phenylserine from glycine and benzaldehyde, both in a tetrahydrofolate-independent reaction, kinetics, cf. EC 4.1.2.48
Products: -
Products: -
-
additional information
?
-
Psychrobacter sp. ANT206
A0A7L7SZS9
Substrates: the enzyme is also active as threonine aldolase, EC 4.1.2.48
Products: -
Products: -
-
additional information
?
-
Substrates: SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
Products: -
Products: -
?
additional information
?
-
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
Substrates: SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
Products: -
Products: -
?
additional information
?
-
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
Psychromonas ingrahamii CCUG 51855
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
Psychromonas ingrahamii DSM 17664
Substrates: using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: L-threonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: D-allothreonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no: L-threonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-serine, but the Ta1509 protein shows significant threonine-cleavage activity with substrates L-threonine and L-allo-threonine, cf. EC 4.1.2.48, but neither D-threonine nor D-allo-threonine serve as substrates
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with D-serine, but the Ta1509 protein shows significant threonine-cleavage activity with substrates L-threonine and L-allo-threonine, cf. EC 4.1.2.48, but neither D-threonine nor D-allo-threonine serve as substrates
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with D-serine, but the Ta1509 protein shows significant threonine-cleavage activity with substrates L-threonine and L-allo-threonine, cf. EC 4.1.2.48, but neither D-threonine nor D-allo-threonine serve as substrates
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with D-serine, but the Ta1509 protein shows significant threonine-cleavage activity with substrates L-threonine and L-allo-threonine, cf. EC 4.1.2.48, but neither D-threonine nor D-allo-threonine serve as substrates
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with D-serine, but the Ta1509 protein shows significant threonine-cleavage activity with substrates L-threonine and L-allo-threonine, cf. EC 4.1.2.48, but neither D-threonine nor D-allo-threonine serve as substrates
Products: -
Products: -
-
additional information
?
-
-
Substrates: review and comparison of enzyme activity, threonine aldolase and allothreonine aldolase activity from various sources
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-Ser
-
Substrates: the enzyme is a major source of one-carbon units for cellular metabolism. Potential for disruption of SHMT-mediated one-carbon metabolism by inadequate vitamin B-6 intake
Products: -
Products: -
r
L-Ser + tetrahydrofolate
Gly + 5,10-methylenetetrahydrofolate
-
Substrates: placental conversion of serine to glycine is a major source of fetal glycine
Products: -
Products: -
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + D-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
(6S)-tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + D-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Aedes aegypti NIH Rockefeller
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
A0A069BAT4
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
A0A069BAT4
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Lathyrus oleraceus Progress 9
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
-
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: regulatory protein
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: main glycine source for purine biosynthetic pathway in ureide biogenesis
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme is a component of thymidylate cycle
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme is a component of thymidylate cycle
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: major pathway for production of C1-units of 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: catalyzes interconversion of serine and glycine
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: enzyme plays a pivotal role in channelling metabolites between amino acid and nucleotide metabolism
Products: -
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L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: may play important role in central nervous system
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: -
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: regulatory protein
Products: -
Products: -
?
L-serine + tetrahydrofolate
glycine + 5,10-methylenetetrahydrofolate + H2O
-
Substrates: key enzyme of serine pathway for assimilation of C1-compounds
Products: -
Products: -
?
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
Substrates: -
Products: -
Products: -
r
L-serine + tetrahydropteroylglutamate
glycine + 5,10-methylene-tetrahydropteroylglutamate + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Aedes aegypti NIH Rockefeller
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei CGMCC 1.3690
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei DSM 16502
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Alloalcanivorax dieselolei MCCC 1A00001
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum CCUG 27702
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum NBRC 12168
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Corynebacterium glutamicum NRRL B-2784
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Glycine max F650
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Mus musculus B6EiC3SnF1/J
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
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Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
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r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychrobacter sp. ANT206
A0A7L7SZS9
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychromonas ingrahamii CCUG 51855
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Psychromonas ingrahamii DSM 17664
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + L-serine
5,10-methylenetetrahydrofolate + glycine + H2O
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
Products: -
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?
additional information
?
-
-
Substrates: SHMT1 functions in the photorespiratory pathway and plays a critical role in controlling the cell damage provoked by abiotic stresses such as high light and salt and in restricting pathogen induced cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
Products: -
Products: -
?
additional information
?
-
Substrates: disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
Products: -
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?
additional information
?
-
-
Substrates: disruption of the SHM2 gene, encoding one of two serine hydroxymethyltransferase isoenzymes, reduces the flux from glycine to serine
Products: -
Products: -
?
additional information
?
-
-
Substrates: SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an indispensable role in nucleic acid biosynthesis
Products: -
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?
additional information
?
-
-
Substrates: low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
Products: -
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additional information
?
-
-
Substrates: Plasmodium SHMT can use D-serine and L-serine as a substrate
Products: -
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additional information
?
-
Substrates: the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
Products: -
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?
additional information
?
-
-
Substrates: the enzyme catalyzes the conversion of L- and D-serine to glycine in a THFdependent reaction
Products: -
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additional information
?
-
-
Substrates: Plasmodium SHMT can use D-serine and L-serine as a substrate
Products: -
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additional information
?
-
-
Substrates: serine hydroxymethyltransferase is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes a hydroxymethyl group transfer from L-serine to tetrahydrofolate to yield glycine and 5,10-methylenetetrahydrofolate
Products: -
Products: -
?
additional information
?
-
Substrates: SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
Products: -
Products: -
?
additional information
?
-
Substrates: SHMT catalyses the reversible cleavage of several beta-hydroxy amino acids varying in substituent and stereochemistry at Cbeta. The enzyme also has L-threo-beta-phenylserine aldolase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: low activity in placenta suggests that placental conversion of serine to glycine is not a major source of fetal glycine
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high serine hydroxymethyltransferase activity and L-serine production
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,10-methylenetetrahydrofolate
-
pyridoxal 5'-phosphate
-
requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
-
dimeric form of some mutant enzymes contains no pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
SHM1 contains 1 mol per mol of enzyme dimer
pyridoxal 5'-phosphate
SHM2 contains 2 mol per mol of enzyme dimer
pyridoxal 5'-phosphate
-
mutant enzymes K226M and K226Q contain 1 mol of pyridoxal 5'-phosphate per mol of subunit. Pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
pyridoxal 5'-phosphate
-
dependent on, the apo enzyme has some enzyme activity in the absence of pyridoxal 5'-phosphate but this activity is only slightly above background and can be due to incomplete removal of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
the Kd for binding of the enzyme and pyridoxal 5'-phosphate is 0.00014 mM
pyridoxal 5'-phosphate
-
wild type enzyme contains 1 mol per mole of subunit
pyridoxal 5'-phosphate
-
dependent on, stabilizes the dimeric form of the enzyme
pyridoxal 5'-phosphate
dependent on, cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
pyridoxal 5'-phosphate
dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
pyridoxal 5'-phosphate
-
dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
pyridoxal 5'-phosphate
-
dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
the amino acid residues composing the PLP-binding site of SHMTs are well conserved in the Ta1509 protein
pyridoxal 5'-phosphate
SHMT is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
pyridoxal 5'-phosphate
SHMT is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
pyridoxal 5'-phosphate
the residues for PLP binding, such as G98, S99, D200, H203, G268, and R368, formed hydrogen interaction with the ligand (PLG), binding structure analysis
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
-
requirement with L-serine or L-2-methylserine as substrate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Mg2+
Mn2+
Zinc
-
within a mimosine-responsive transcriptional element localized within the first 50 base pairs of the human SHMT1 promoter, 50-base-pair sequence contains a consensus zinc-sensing metal regulatory element at position -44 to -38
additional information
additional information
-
Mg2+, K+, Na+and EDTA have no significant effect on the enzyme activity
additional information
no effects on enzyme activity by K+ and Ni2+
additional information
-
K+, Na+ and NH4+ show no appreciable impact on the SHMT activity
additional information
K+, Na+, NH4+, Mg2+, Ca2+, Zn2+ and Pb2+ show no significant effect on enzyme activity
additional information
-
K+, Na+, NH4+, Mg2+, Ca2+, Zn2+ and Pb2+ show no significant effect on enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+/-)-methyl 5-[3-(6-amino-5-cyano-4-isopropyl-3-methyl-1,4-dihydropyrano[2,3-c]pyrazol-4-yl)-5-cyanophenyl]thiophene-2-carboxylate
-
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
(6-amino-1,4-dihydro-4-[5-(hydroxymethyl)[1,1'-biphenyl]-3-yl]-3-methyl-4-(1-methylethyl)pyrano[2,3-c]pyrazole-5-carbonitrile
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
3-Bromopyruvate
isoform SHMT1 is completely inhibited by 3-bromopyruvate; isoform SHMT2 retains a significant fraction of activity with 3-bromopyruvate
5-formyltetrahydrofolate
-
can inhibit SHMT in vivo and thereby influence glycine pool size, can accumulate glycine in both wild-type and 5-CHO-THF cycloligase mutant
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
6-amino-1,4-dihydro-4-[5-(hydroxymethyl)[1,1'-biphenyl]-3-yl]-3-methyl-4-(1-methylethyl)pyrano[2,3-c]pyrazole-5-carbonitrile
serine hydroxymethyltransferase inhibitor 1 (SHIN1)
6-amino-3-(2-chlorophenyl)-4-(3,4-dimethoxyphenyl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-3-(4-fluorophenyl)-4-(naphthalen-1-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-(3,5-dimethoxyphenyl)-3-(4-methoxyphenyl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
6-amino-4-[3-cyano-5-(piperazin-1-yl)phenyl]-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitril
-
-
6-amino-4-[3-cyano-5-(piperazin-1-yl)phenyl]-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
Antibodies to mitochondrial enzyme
-
no inhibition of cytosolic enzyme
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
L-mimosine
-
inhibits SHMT1 transcription by chelating zinc, eliminates the metal regulatory element- and Sp1-binding activity in nuclear extracts from MCF-7 cells, but not in nuclear extracts from the mimosine-resistant cell line, MCF-7/2a
leucovorin
leucovorin (N5-CHO-THF) exhibits a differential inhibition pattern: it significantly inhibits the aldol cleavage of serine catalyzed by zebrafish cytosolic SHMT but it inhibits to a lesser extent the reaction catalyzed by the mitochondrial isozyme. Approximately 70% and 30% inhibition are observed for zebrafish cytosolic- and zebrafish mitochondrial SHMT activities, respectively, in the presence of 70 mM leucovorin. An even larger difference between both isoenzymes is observed when the inhibition is assayed in the presence of 50 mM serine; leucovorin (N5-CHO-THF) exhibits a differential inhibition pattern: it significantly inhibits the aldol cleavage of serine catalyzed by zebrafish cytosolic SHMT but it inhibits to a lesser extent the reaction catalyzed by the mitochondrial isozyme. Approximately 70% and 30% inhibition are observed for zebrafish cytosolic- and zebrafish mitochondrial SHMT activities, respectively, in the presence of 70 mM leucovorin. An even larger difference between both isoenzymes is observed when the inhibition is assayed in the presence of 50 mM serine
mangiferin
analysis of mangiferin interactions in the enzyme binding site, modelling, overview
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
methyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
N-[4-[3-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)propyl]-2-fluorobenzoyl]-L-glutamic acid
-
N-[4-[3-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)propyl]benzoyl]-L-glutamic acid
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamyl-gamma-glutamylglutamic acid
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamylglutamic acid
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]glutamic acid
-
N-[4-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]-2-fluorobenzoyl]-L-glutamic acid
-
N-[5-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]-3-fluorothiophene-2-carbonyl]-L-glutamic acid
-
N-[5-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]thiophene-2-carbonyl]-L-glutamic acid
-
SHIN1
a SHMT2 inhibitor. High SHMT2-expressing RMS cells are less sensitive to the SHMT inhibitor SHIN1
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
-
-
(4R,4S)-5-cyano-4-(3-cyano-5-[5-[((S)-1,3-dicarboxypropyl)-carbamoyl]thiophen-2-yl]phenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-6-aminium trifluoroacetate
-
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
-
-
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N-[3-(diethylamino)propyl]thiophene-2-carboxamide
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
-
-
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylic acid
-
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
-
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
-
-
6-amino-5-cyano-4-[3-cyano-5-(5-[[3-(morpholin-4-ium-4-yl)propyl]carbamoyl]thiophen-2-yl)phenyl]-3-methyl-4-isopropyl-2,4-dihydropyrano[2,3-c]pyrazol-1-ium bis-(trifluoroacetate)
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
-
-
benzyl 4-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]piperazine-1-carboxylate
-
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
Bromopyruvate
-
irreversible inactivation, substrates partially protect
Chloroacetaldehyde
-
irreversible inactivation, substrates partially protect
Cibacron blue F3GA
-
complete inhibition, NAD(H) protects, reversible by tetrahydrofolate
D-alanine
-
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-alanine
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-alanine
-
inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction
D-cycloserine
-
overexpression of SHMT-S increases resistance in a rich folate containing medium
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
-
-
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
-
glycine
-
glycine inhibits His6-tagged SHMT competitively with respect to serine and non-competitively with respect to tetrahydrofolate
iodoacetamide
-
irreversible inactivation, substrates partially protect
L-amino acids
-
weak, e.g. L-aspartic acid, ornithine, lysine, methionine, phenylalanine, homoserine, threonine, 4-aminobutyric acid
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
-
-
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
-
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
-
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
-
NaCl
60% inhibition at 100 mM, restored to 66-71% activity in presence of 50 mM glycine betaine
NaCl
the enzyme activity is salt sensitive, overview. The highest kcat value is shown in the absence of salt
NaCl
the enzyme activity is salt sensitive, overview. The highest kcat value is shown in the absence of salt
pemetrexed
-
i.e. (S)-2-[4-[2-(4-amino-2-oxo-3,5,7-triazabicyclo[4.3.0]nona-3,8,10-trien-9-yl) ethyl] benzoyl]aminopentanedioic acid, brand name Alimta, low micromolar inhibitor
tetrahydrofolate
-
strong and pH-dependent substrate inhibition due to the formation of the enzyme-glycine:tetrahydrofolate dead-end complex (at low pH values)
tetrahydrofolate
isoform SHMT2 maintains a pronounced tetrahydrofolate substrate inhibition even at the alkaline pH characteristic of the mitochondrial matrix
tetrahydrofolate
inhibitory at non-saturating concentration of serine, at concentrations above 1.5 mM
tetrahydrofolate
at concentrations above 0.015 mM, substrate inhibition is observed
Thiosemicarbazide
-
poorly active against promastigotes, but SHMT-S transfectants can provide a small but significant resistance
Urea
in 1 M urea, almost all the cofactor is bound to the enzyme as internal aldimine, indicating that the loss of activity does not result from the denaturation of the active site, these observations suggest that urea might act as an enzyme inhibitor
additional information
model of uncompetitive substrate inhibition using tetrahydropteroylglutamates with different numbers of glutamate residues, overview
-
additional information
-
model of uncompetitive substrate inhibition using tetrahydropteroylglutamates with different numbers of glutamate residues, overview
-
additional information
compound library screening against SHMT
-
additional information
-
not: ethanolamine, ethylenediamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
-
not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
the enzyme is not significantly influenced in activity by NH4+, Sl2+, Ca2+, Pb2+, SDS and CTAB
-
additional information
-
the enzyme is not significantly influenced in activity by NH4+, Sl2+, Ca2+, Pb2+, SDS and CTAB
-
additional information
-
not: methionine, S-adenosyl-L-methionine, XMP, IMP, phosphoglycerate
-
additional information
prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
additional information
5-substituted pyrrolo[3,2-d]pyrimidine antifolate inhibitors inhibit the human serine hydroxymethyl transferase 2 resulting in potent in vitro and in vivo antitumor efficacies, enzyme in complex with with an expanded series of pyrrolo[3,2-d]pyrimidine compounds with variations in bridge length (3?5 carbons) and the side chain aromatic ring (phenyl, thiophene, fluorine-substituted phenyl, and thiophene), binding structure and kinetics analysis, influence of antifolate polyglutamylation on SHMT2:inhibitor interactions, overview
-
additional information
virtual screening identifies 27 candidates as enzyme inhibitors of which three compounds feature medium-strength and non-competitive inhibition of SHMT2. Evaluation of a quick screening method for the identification of inhibitors targeting SHMT2, inhibitors docking, mode of inhibition of SHMT2, overview
-
additional information
-
not: NaN3, mono- or divalent cations, 2-mercaptoethanol, DTT; not: iodoacetate; not: purine nucleoside mono-, di- and triphosphates
-
additional information
-
not: N-/O-chloroacetyl and N-/O-bromoacetyl derivatives of glycine and L-serine
-
additional information
-
in order to act as selective ligands for the active site, the tails of the 5-formyl-6-hydrofolic acid analogues as potential selective inhibitors should be short to avoid the repulsive interactions with residues Lys138, Lys139 and Lys140 of the active site of SHMT, the tails may be longer, but in that case they must possess both negative and positive charges at the right positions, in order to explore their interactions with Lys138, Lys139, Lys140 and Glu137, prototypes with negative total charge have greater affinity for Plasmodium falciparum SHMT than for human SHMT
-
additional information
-
not: mercaptopropionic acid, mercaptoethanolamine; not: valine, leucine, glutamic acid, 3-hydroxybutyric acid
-
additional information
-
not: EDTA; not: purine nucleoside mono-, di- and triphosphates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,6,7,8-tetrahydrofolate
-
control of SHMT activity by the availability of 5,6,7,8-tetrahydrofolate
glycine-betaine
addition of the osmoprotectant glycine betaine under salt conditions has a distinct positive effect on AhSHMT activity
glycine-betaine
addition of the osmoprotectant glycine betaine under salt conditions has a distinct positive effect on AhSHMT activity
additional information
Q2TL58
higher concentrations of IPTG, increased induction temperature and/or prolonged induction time increase the ratio of insoluble and soluble SHMT-1
-
additional information
-
higher concentrations of IPTG, increased induction temperature and/or prolonged induction time increase the ratio of insoluble and soluble SHMT-1
-
additional information
-
recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis
-
additional information
-
in the presence of 1mM dithiothreitol + 1mM pyridoxal 5-phosphate + 20 mM EDTA: 29fold increase in the specific activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with L-serine in HEPES buffer
0.007
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with L-serine in phosphate buffer
0.021
(6S)-tetrahydrofolate
pH 7.0, 25°C, recombinant enzyme, with D-serine
0.2
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme
0.22
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.22
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.23
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.27
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.29
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.291
5,10-methylenetetrahydrofolate
isoform SHMT1, at pH 8.8 and 30°C
0.35
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.42
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.43
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.98
5,10-methylenetetrahydrofolate
isoform SHMT2, at pH 8.8 and 30°C
0.071
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C
57.86
DL-3-phenylserine
wild type enzyme, at pH 7.8 and 30°C
61.95
DL-3-phenylserine
mutant enzyme I249L, at pH 7.8 and 30°C
0.49
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.85
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.9 - 1
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
1
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
1.18
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
1.22
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
2.29
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
5.87
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
0.00436
L-serine
pH 7.4, 40°C, recombinant mutant E160L/E193Q
0.01038
L-serine
pH 7.4, 40°C, recombinant wild-type enzyme
0.14
L-serine
apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.15
L-serine
apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.2
L-serine
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.24
L-serine
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
0.29
L-serine
pH and temperature not specified in the publication
0.3
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
0.31
L-serine
-
pH and temperature not specified in the publication
1.13
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
1.5 - 2
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
1.93
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
2.06
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
2.22
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
4.14
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
5.47
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
8.97
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
11
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
20.66
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
0.003
tetrahydrofolate
-
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C
0.0031
tetrahydrofolate
-
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C
0.00435
tetrahydrofolate
apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.005
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
0.00703
tetrahydrofolate
apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.00716
tetrahydrofolate
apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.011
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
0.0112
tetrahydrofolate
apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
0.014
tetrahydrofolate
-
mutant enzyme H132A, in the presence of NADP+, at pH 3.0 and 30°C
0.018
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
0.02
tetrahydrofolate
apparent value, isoform SHMT1, at pH 7.2 and 20°C
0.023
tetrahydrofolate
apparent value, isoform SHMT2, at pH 7.2 and 20°C
0.03
tetrahydrofolate
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
0.038
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
0.042
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
0.048
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
0.049
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
0.051
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
0.054
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
0.055
tetrahydrofolate
-
wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C
0.06
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.065
tetrahydrofolate
-
pH and temperature not specified in the publication
0.086
tetrahydrofolate
pH and temperature not specified in the publication
0.09
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.094
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
0.1
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.1 - 1
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.1 - 1
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.13
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.14
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.2177
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
0.22
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
0.25
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.37
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
0.89
tetrahydrofolate
-
wild-type, in the presence of 0.25 mM pyridoxal phosphate
1.16
tetrahydrofolate
-
mutant K251R, in the presence of 0.25 mM pyridoxal phosphate
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
kinetic analysis of ternary complex mechanism, determination of ligand binding, transient, single-turnover and bi-substrate steady-state kinetics, detailed overview. The enzyme can bind first to either L-serine or tetrahydrofolate. The dissociation constants for the enzyme-L-serine and enzyme-tetrahydrofolate complexes are 0.18 mM and 0.35 mM, respectively. The kinetic mechanism of PvSHMT occurs via a random-order model and glycine formation is the rate-limiting step of the enzyme reaction
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
Michaelis-Menten kinetics, steady-state kinetics in absence of presence of NaCl and at different pH values, overview
-
additional information
additional information
Michaelis-Menten kinetics, steady-state kinetics in absence of presence of NaCl and at different pH values, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.158
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.168
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.17
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.193
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.195
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme
0.202
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.213
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.22
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme
0.225
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.23
5,10-methylenetetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.246
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C
4.8
DL-3-phenylserine
mutant enzyme I249L, at pH 7.8 and 30°C
0.158
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
0.168
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.17
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.193
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.202
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.213
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.225
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.23
glycine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
6.7
L-serine
mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
6.7
L-serine
mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
8.1
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
10.8
L-serine
mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
11.4
L-serine
wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA
14
L-serine
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
15.83
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
21.52
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
21.83
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
27.33
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
28.5
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
39.52
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl
46.57
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
56.63
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
65.37
L-serine
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
640
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
0.033
tetrahydrofolate
mutant L474F, in the presence of pyridoxal phosphate
0.045
tetrahydrofolate
mutant S394N, in the presence of pyridoxal phosphate
0.07
tetrahydrofolate
wild-type, in the presence of pyridoxal phosphate
0.41
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
0.57
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
0.81
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
1.1
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
1.13
tetrahydrofolate
-
mutant K251R, in the presence of 0.25 mM pyridoxal phosphate
1.3
tetrahydrofolate
-
wild-type, in the presence of 0.25 mM pyridoxal phosphate
1.41
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
8.1
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
14
tetrahydrofolate
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
15.8
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
15.83
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
21.52
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
21.83
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
27.33
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
28.5
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
39.52
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
46.57
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
56.63
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
65.37
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.52
5,10-methylenetetrahydrofolate
isoform SHMT2, at pH 8.8 and 30°C
0.65
5,10-methylenetetrahydrofolate
isoform SHMT1, at pH 8.8 and 30°C
0.00346
D-serine
-
apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C
0.028
DL-3-phenylserine
wild type enzyme, at pH 7.8 and 30°C
0.077
DL-3-phenylserine
mutant enzyme I249L, at pH 7.8 and 30°C
0.00065
L-serine
-
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C
0.00071
L-serine
-
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C
35.5
L-serine
-
wild-type enzyme, pH and temperature not specified in the publication
58.33
L-serine
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
1087.2
L-serine
pH 7.4, 40°C, recombinant mutant E160L/E193Q
0.011
tetrahydrofolate
-
mutant enzyme H132A, in the presence of NADP+, at pH 3.0 and 30°C
0.047
tetrahydrofolate
-
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C
0.074
tetrahydrofolate
-
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C
0.081
tetrahydrofolate
-
wild type enzyme, in the presence of NADP+, at pH 3.0 and 30°C
11
tetrahydrofolate
-
at pH 8.3, temperature not specified in the publication
14
tetrahydrofolate
-
at pH 7.9, temperature not specified in the publication
15
tetrahydrofolate
-
at pH 7.5, temperature not specified in the publication
22
tetrahydrofolate
-
at pH 6.6, temperature not specified in the publication
29
tetrahydrofolate
-
at pH 7.1, temperature not specified in the publication
70
tetrahydrofolate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
466.67
tetrahydrofolate
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00045
(6-amino-1,4-dihydro-4-[5-(hydroxymethyl)[1,1'-biphenyl]-3-yl]-3-methyl-4-(1-methylethyl)pyrano[2,3-c]pyrazole-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.00046
N-[4-[3-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)propyl]-2-fluorobenzoyl]-L-glutamic acid
pH 7.5, temperature not specified in the publication
0.00034
N-[4-[3-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)propyl]benzoyl]-L-glutamic acid
pH 7.5, temperature not specified in the publication
0.000024
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
pH 7.5, temperature not specified in the publication
0.00046
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamyl-gamma-glutamylglutamic acid
pH 7.5, temperature not specified in the publication
0.00016
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]-gamma-glutamylglutamic acid
pH 7.5, temperature not specified in the publication
0.00045
N-[4-[4-(2-amino-4-oxo-3,4-dihydro-5H-pyrrolo[3,2-d]pyrimidin-5-yl)butyl]-2-fluorobenzoyl]glutamic acid
pH 7.5, temperature not specified in the publication
0.000016
N-[4-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]-2-fluorobenzoyl]-L-glutamic acid
pH 7.5, temperature not specified in the publication
0.00063
N-[5-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]-3-fluorothiophene-2-carbonyl]-L-glutamic acid
pH 7.5, temperature not specified in the publication
0.00006
N-[5-[5-(2-amino-4-methyl-5H-cyclopenta[d]pyrimidin-5-yl)pentyl]thiophene-2-carbonyl]-L-glutamic acid
pH 7.5, temperature not specified in the publication
0.085
tetrahydropteroylglutamate
pH 8.5, temperature not specified in the publication, recombinant AtSHMT3
0.1
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.12
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.13
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.17
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl
0.17
tetrahydrofolate
pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex
0.18
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.25 M NaCl
0.18
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl
0.18
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.19
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.5 M NaCl
0.23
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
0.29
tetrahydrofolate
pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl
additional information
additional information
-
comparison of Ki for allothreonine and threonine
-
additional information
additional information
inhibition kinetic analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000009
(+/-)-methyl 5-[3-(6-amino-5-cyano-4-isopropyl-3-methyl-1,4-dihydropyrano[2,3-c]pyrazol-4-yl)-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium berghei
-
at pH 7.0, temperature not specified in the publication
0.00037
(4R)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00047
(4S)-6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00022
3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-cyano[1,1'-biphenyl]-3-carboxylic acid
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00027
5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]-N,N-dimethylthiophene-2-carboxamide
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00048
6-amino-3-methyl-4-[3-(morpholin-4-yl)-5-(trifluoromethyl)phenyl]-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00029
6-amino-4-(3,5-dichlorophenyl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00021
6-amino-4-(5-cyano-3'-fluoro[1,1'-biphenyl]-3-yl)-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00017
benzyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00042
benzyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00056
ethyl 4-[[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl](methyl)amino]butanoate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.5
methotrexate
Plasmodium falciparum
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37°C
0.00021
methyl 3'-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5'-chloro[1,1'-biphenyl]-4-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00542
methyl 5-[3-[(4R)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00006
methyl 5-[3-[(4S)-6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.00037
methyl 5-[3-[6-amino-5-cyano-3-methyl-4-(propan-2-yl)-2,4-dihydropyrano[2,3-c]pyrazol-4-yl]-5-cyanophenyl]thiophene-2-carboxylate
Plasmodium falciparum
-
at pH 7.0, temperature not specified in the publication
0.5
pyrimethamine
Plasmodium falciparum
-
IC50 above 0.5 mM, in 50 mM Tris-HCl pH 8.0, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0385
-
in the presence of glycine, in 200 mM HEPES buffer, pH 7.0
0.05
-
mutant enzyme Y61A, using L-serine as substrate, at 37°C
0.16
0.5
pH 7.2, 37°C, extract from Escherichia coli cells carrying the expression vector
0.6
1.86
-
after 3.8fold purification, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25°C
10
4.2
4.3
additional information
0.16
-
crude extract, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25°C
additional information
-
maximal activity of 6.3 U/mg total protein is reached
additional information
isolated protein possesses functional activity as transformation into glycine auxotroph GS245 Escherichia coli shows that only pvshmt-transformed cells are able to complement the growth whereas the control cells require glycine supplementation
additional information
-
isolated protein possesses functional activity as transformation into glycine auxotroph GS245 Escherichia coli shows that only pvshmt-transformed cells are able to complement the growth whereas the control cells require glycine supplementation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.2
7.5
7.8
8.5
additional information
additional information
-
pI, cytosolic enzyme: 4.5, pI, mitochondrial enzyme: 4.8
additional information
-
pI, cytosolic enzyme: 4.95, pI, mitochondrial enzyme: 5.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 4
-
about 60% activity at pH 2.0, 100% activity at pH 3.0, about 20% activity at pH 4.0
4 - 10
5 - 10
5.5 - 9.5
5.8 - 9
almost inactive at pH 5.8, less than 10% of maximal activity at pH 6.0, maximal activity at pH 8.0, 80% of maximal activity at pH 7.5 and pH 8.5, inactive at pH 9.5
6 - 10
6 - 8.5
-
cytosol: about 60% of maximal activity at pH 6, about 70% at 8.5, mitochondria: about 40% of maximal activity at pH 6.0 and 8.5
6.6 - 8.4
-
the catalytic efficiency of the enzyme for tetrahydrofolate is about 29fold greater at pH 6.6 than at pH 8.3
7 - 10
-
about 20% activity at pH 6.5, about 85% activity at pH 7.0, about 95% activity at pH 8.0, about 75% activity at pH 9.0, about 45% activity at pH 10.0
7 - 8
the enzyme shows more than 40% activity between pH 7.0 and 8.0. The enzyme displays less than 20% of its maximal activity at pH 5.5 and nearly no activity is detected below pH 2.5
7 - 9
-
serine synthesis: about 80% of maximal activity at pH 7.0 and 9.0
7.2 - 8.6
-
3-phenylserine degradation: about half-maximal activity at pH 7.2 and 8.6
7.3 - 9.5
-
about half-maximal activity at pH 7.3 and about 60% of maximal activity at 9.5
4 - 10
activity range, profile overview. High activity at pH 6.0-8.5
5.5 - 9.5
maximal activity at pH 7.0, 88% of the maximal activity at pH 7.0-8.0, less than 20% of maximal activity at pH 9.5, nearly no activity below pH 5.5
6 - 10
activity range, profile overview. High activity at pH 6.5-8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
30
37
40
45
50
60
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
Psychrobacter sp. ANT206
A0A7L7SZS9
activity range, profile overview. Cold-adapted SHMT, rPsSHMT also shows a high kcat value and low DELTAG at low temperatures
29 - 42
-
serine synthesis, about half-maximal activity at 28.5°C and 90% of maximal activity at 42°C
30 - 42
-
2-phenylserine degradation, about half-maximal activity at 29.5°C and 80% of maximal activity at 42°C
30 - 65
the enzyme retains over 50% of the maximal activity at 30-65°C
30 - 70
5 - 45
60% of maximal activity at 30°C and 45°C, rapid loss of activity above
additional information
additional information
the cold-adaptation mechanism of serine hydroxymethyltransferase is analyzed by comparative molecular dynamics simulations
additional information
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of hcSHMT still remains active below the temperature breakpoint
additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of hcSHMT still remains active below the temperature breakpoint
additional information
enzyme is thermally stable up to 45°C where it exhibits 85% activity. At 65°C it loses its activity
additional information
-
enzyme is thermally stable up to 45°C where it exhibits 85% activity. At 65°C it loses its activity
additional information
-
thermograms of enzyme and mutant enzyme in the absence and presence of L-serine
additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of human cytosolic SHMT still remains active below the temperature breakpoint
additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of human cytosolic SHMT still remains active below the temperature breakpoint
additional information
the cold-adaptation mechanism of serine hydroxymethyltransferase is analyzed by comparative molecular dynamics simulations
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
441393, 441416, 441420, 441425, 441426, 441427, 441428, 441429, 441430, 441434, 657811, 658892, 659572, 719472
-
-
brenda
Psychrobacter sp. ANT206
cf. 4.1.2.48; isolated from the Antarctic sea ice (68°30' E, 65°00' S)
A0A7L7SZS9
UniProt
brenda
cv. Solara, antisense lines G310-10, G310-16, G310-76, G310-101 and G310-106
-
-
brenda
lysostaphin-susceptibel strain USA300 and and lysostaphin-resistant sequence type 72, the latter is isolated from a patient in whom the Staphylococcus aureus infection is highly resistant to various antibiotics and lysostaphin
SwissProt
brenda
SCN-susceptible cv. Essex and SCN-resistant cv. Forrest
UniProt
brenda
strain GM2, a glycine resistant mutant derived from strain KM146
-
-
brenda
-
-
-
brenda
one enzymatically functional SHMT isozyme, PfSHMTc, and one related, apparently inactive isoform, PfSHMTm, encoded by different genes pfshmt and PF14_ 0534, respectively
-
-
brenda
lysostaphin-susceptibel strain USA300 and and lysostaphin-resistant sequence type 72, the latter is isolated from a patient in whom the Staphylococcus aureus infection is highly resistant to various antibiotics and lysostaphin
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme expression in samples from different carcinomas from different tissues and origins, overview
brenda
analysis of shmt1 expression in patients during lung cancer progression
brenda
-
both PfSHMTc and PfSHMTm are concentrated in the central region of the parasite that becomes the residual body on erythrocyte lysis and merozoite release
brenda
serine hydroxymethyltransferase 2 (SHMT2) protein is overexpressed at the protein level in an amplicon-positive rhabdomyosarcoma (RMS) cell line
brenda
-
early trophozoites lack visible organellar isozyme PfSHMTc, while it occurs during the mid-to-late trophozoite and schizont stages
brenda
-
protoxylem and/or adjacent cells, SHM1 and SHM2
brenda
additional information
SHMT2 is overexpressed in human aggressive B-cell lymphomas
brenda
elevated SHMT2 expression in aggressive murine MYC-induced lymphomas
brenda
in healthy brains, SHMT2 expression is not detected in most cells but is at low levels in astrocytes and vessels
brenda
-
expression patterns of SHMT2 in 76 breast cancer patients after modified radical mastectomy, immunohistochemic analysis, SHMT2 is highly expressed in breast cancer cells, and the expression level of SHMT2 is positively correlated with breast cancer grade
brenda
in human glioblastoma multiforme, mitochondrial serine hydroxymethyltransferase (SHMT2) and glycine decarboxylase are highly expressed in the pseudopalisading cells that surround necrotic foci
brenda
endoplasmic reticulum stress-dependent regulation of the expression of serine hydroxymethyltransferase 2 in glioblastoma cells
brenda
-
SHMT activity of antisense lines is 70-90% lower than in the wild-type, negative effects of antisensed SHMT becomes increasingly severe with plant age
brenda
siginificant protein expression detected by Western Blotting only in liver and ovary
brenda
elevated mRNA expression detected by RT-PCT. Strong protein expression detected by western blotting
brenda
-
from rats fed dietary pyridoxine ranging from adequare to deficient levels, 2-0 mg pyridoxine per kg diet
brenda
-
inoculated with Rhizobium japonicum strain 311b142
-
brenda
siginificant protein expression detected by Western Blotting only in liver and ovary
brenda
elevated mRNA expression detected by RT-PCT. Strong protein expression detected by western blotting
brenda
-
low activity, activity is similar 8 weeks post conception and at term
brenda
-
activity per gram of placenta increases 2.1fold between midgestation and term
brenda
additional information
-
cellular distribution of SHM1 and SHM2, detailed overview
brenda
additional information
RT-PCR results show that zmSHMT mRNA is evenly distributed among tissues. However zmSHMT protein expression does not correspond to the detected mRNA expression detected in most tissues
brenda
additional information
RT-PCR results show that zmSHMT mRNA is evenly distributed among tissues. However zmSHMT protein expression does not correspond to the detected mRNA expression detected in most tissues
brenda
additional information
-
RT-PCR results show that zmSHMT mRNA is evenly distributed among tissues. However zmSHMT protein expression does not correspond to the detected mRNA expression detected in most tissues
brenda
additional information
-
SHMT2alpha co-localizes with lamin B1 in SH-SY5Y cells. Recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis
brenda
additional information
enzyme SHMT2 is highly expressed in many fast-growing cancer cells
brenda
additional information
gene is preferentially expressed in the amastigote stage of parasite
brenda
additional information
-
gene is preferentially expressed in the amastigote stage of parasite
brenda
additional information
-
gene is preferentially expressed in the amastigote stage of parasite
-
brenda
additional information
Psychrobacter sp. ANT206
A0A7L7SZS9
the strain is cultured at pH 7.5 and 12°C
brenda
additional information
the Ta1509 protein is not stable at 85°C and can be obtained only at a lower cultivation temperature
brenda
additional information
-
the Ta1509 protein is not stable at 85°C and can be obtained only at a lower cultivation temperature
-
brenda
additional information
-
the Ta1509 protein is not stable at 85°C and can be obtained only at a lower cultivation temperature
-
brenda
additional information
-
the Ta1509 protein is not stable at 85°C and can be obtained only at a lower cultivation temperature
-
brenda
additional information
-
the Ta1509 protein is not stable at 85°C and can be obtained only at a lower cultivation temperature
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isozyme PfSHMTc in a stage-specific manner, isozyme PfSHMTc localization in this organelle is less restricted than for the mitochondrion and persists from the late trophozoite to the post-mitotic stages
brenda
-
enzyme possesses a putative N-terminal hydrogenosomal presequence
brenda
additional information
-
SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses
brenda
-
-
brenda
zcSHMT is detected in the cytosol as well as in the nucleus
brenda
-
from rat liver fed dietary pyridoxine ranging from adequate to deficient levels, 2-0 mg pyridoxine per kg diet. SHMT activity increases with increasing dietary pyridoxine concentrations
brenda
peptide sequence alignment with the known SHMT from other species and the prospective zebrafish cytosolic SHMT as well as signal prediction software reveals a potential mitochondrial signal peptide cleavage site between residues 20 and 30
brenda
-
SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses
brenda
-
isozyme PfSHMTc in a stage-specific manner. Isozyme PfSHMTm showa a distinctly more pronounced mitochondrial location through most of the erythrocytic cycle, presence of a mitochondrial signal sequence
brenda
-
from rat liver fed dietary pyridoxine ranging from adequate to deficient levels, 2-0 mg pyridoxine per kg diet. SHMT activity increases with increasing dietary pyridoxine concentrations. The mitochondrial isoenzyme comprises about 70% of the total activity
brenda
zcSHMT is detected in the cytosol as well as in the nucleus
brenda
-
SHMT1 localizes to the nucleus in response to UV treatment
brenda
-
SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses. SHMT1, SHMT2alpha, thymidylate synthase, and dihydrofolate reductase are present in nuclei during S and G2/M phases
brenda
additional information
-
SHMT-L in an organelle that has hallmarks of the parasite mitochondrion
-
brenda
additional information
-
comparison of cytosolic and mitochondrial forms of enzyme
-
brenda
additional information
-
patterns of localization of the two isoforms during the parasite erythrocytic cycle, overview. Both PfSHMTc and PfSHMTm are concentrated in the central region of the parasite that becomes the residual body on erythrocyte lysis and merozoite release
-
brenda
additional information
-
comparison of cytosolic and mitochondrial forms of enzyme
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
-
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
the enzyme belongs to the fold type-I superfamily of PLP-dependent enzymes
evolution
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
-
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
-
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
-
the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
A0A069BAT4
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
evolution
serine hydroxymethyltransferase (SHMT) and threonine aldolase are classified as fold type I pyridoxal-5'-phosphate-dependent enzymes
evolution
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
evolution
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
evolution
serine hydroxymethyltransferase (SHMT) is a ubiquitous enzyme belonging to the fold type I or aspartate aminotransferase (AspAT) family of the pyridoxal 5'-phosphate (PLP)-dependent enzymes
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
serine hydroxymethyltransferase (SHMT) and threonine aldolase are classified as fold type I pyridoxal-5'-phosphate-dependent enzymes
-
evolution
-
serine hydroxymethyltransferase (SHMT) and threonine aldolase are classified as fold type I pyridoxal-5'-phosphate-dependent enzymes
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
-
evolution
-
the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes
-
evolution
-
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
-
evolution
-
serine hydroxymethyltransferase (SHMT) and threonine aldolase are classified as fold type I pyridoxal-5'-phosphate-dependent enzymes
-
evolution
-
serine hydroxymethyltransferase (SHMT) and threonine aldolase are classified as fold type I pyridoxal-5'-phosphate-dependent enzymes
-
evolution
Psychromonas ingrahamii DSM 17664
-
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
-
evolution
Psychromonas ingrahamii CCUG 51855
-
serine hydroxymethyltransferase (SHMT) belongs to the aspartate aminotransferase superfamily (fold type I) and is a pyridoxal phosphate (PLP or vitamin B6)-dependent enzyme
-
malfunction
-
Shmt1 null mice are fertile and do not demonstrate maternal lethality
malfunction
-
a shm1 null mutant requires CO2-enriched air to inhibit photorespiration, while a shm2 null mutant does not show any visible impairment, a double-null mutant cannot survive in CO2-enriched air. Residual SHM activity is undetectably low in purified leaf mesophyll mitochondria of the shm1 mutant. In roots, the knockout of SHM1 does not reduce total SHM activity, whereas the knockout of SHM2 significantly lowers total SHM activity
malfunction
overexpression of mitochondrial serine hydroxymethyltransferase assures an adequate supply of glycine to rapidly proliferating cancer cells, silencing of mitochondrial serine hydroxymethyltransferase halts cancer cell proliferation and supplementation with sarcosine (a glycine-related metabolite) or formate (a source of one carbon units) fails to rescue cell proliferation
malfunction
suppression of SHMT2 decreases both net serine consumption and glycine production in LN229 cells and completely prevents glycine cleavage activity in isolated mitochondria. The preemptive knockdown of SHMT2 protects BT145, LN229, and U251 cells against the detrimental effects of GLDC knockdown
malfunction
-
a shm1mutant has chlorotic lesions and a considerably smaller, lethal phenotype under natural ambient CO2 concentrations, but can be restored to wild type with normal growth under elevated CO2 levels (0.5% CO2), showing a typical photorespiratory phenotype
malfunction
-
digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
malfunction
inhibition of serine or glycine uptake from the extracellular milieu, as well as knockdown of the cytosolic one-carbon metabolism enzyme serine hydroxymethyltransferase (SHMT1), abolishes migration of lung adenocarcinoma (LUAD) cells
malfunction
defects in one-carbon metabolism lead to severe developmental defects, such as neural tube defects. Shmt is important for larval optic lobe development, with the loss of shmt in the neuroepithelia leading to morphologically abnormal optic lobes, with smaller and defective neuroepithelia in the OPC. As knockdown or knockout (KO) of shmt specifically in the neuroepithelia fully recapitulates the optic lobe phenotype of animals mutant for shmt, this tissue is identified as the origin of the phenotype. Increased levels of apoptosis in the neuroepithelia partly explain their reduced size and the reduction in the number of neuroblasts (NBs) and medulla neurons. In addition, shmt mutant neuroepithelia do not form a lamina furrow, a structure essential for the formation of lamina neurons. Consistently, in shmt-depleted optic lobes there are no lamina neurons. Mechanisms that lead to a defective optic lobe in shmtm3-5 animals, overview
malfunction
mutant DELTAshmT is susceptible to the lysostaphin, while complementation of the knockout expressing shmT restores resistance against lysostaphin. In addition, the DELTAshmT shows reduced virulence under in vitro (mammalian cell lines infection) and in vivo (wax-worm infection) models. The SHMT inhibitor, serine hydroxymethyltransferase inhibitor 1 (SHIN1), protects the 50% of the wax-worm infected with wild type Staphylococcus aureus
malfunction
-
the low level of cysteine-rich proteins (lcrp) mutation indicates a decrease in cysteine-rich (CysR) prolamines, alpha-globulin, and glutelin. The levels of L-Ser, Gly, and Met in the sulfur assimilation pathway in the lcrp seeds increase significantly compared to that in the wild-type. The lcrp mutation influences the growth of shoot and root. Accumulation of cysteine-poor prolamines in the lcrp seeds. Glutelin-containing protein bodies (PBs) are smaller and distorted in the lcrp seeds compared to those in the wild-type
malfunction
the P285S substitution decreases stability of the SHMT8 tetramer, increases protein flexibility and reduces thermal stability
malfunction
the expression level of the SHMT2 gene is affected by ERN1 knockdown and is very sensitive to glucose and glutamine deprivation in U87MG glioblastoma cells in an ERN1-dependent manner, role of the endoplasmic reticulum stress signaling mediated by ERN1 in the regulation of SHMT2 gene expression in glioblastoma cells, overview
malfunction
mutation of SHMT1 clearly exhibit chlorotic and lethal phenotypes under ambient growth conditions, which are rescued by elevated CO2 and partially by GSH. Mutant shm1-2 exhibits a severe root-retardation phenotype at low-sucrose conditions with increased H2O2 levels, and plants with SHMT1 overexpression have longer roots with reduced H2O2 levels. Sugar-feeding assays, ROS scavenging by GSH, or reduction of RBOHD expression partially restore the root-growth inhibition phenotype at low-sucrose conditions. Exogenous sucrose rescued the root-growth-arrest phenotype of shm1-2 mutant, but elevated CO2 alone does not, overview
malfunction
enzyme SHMT8 from Glycine max cv. Forrest has a severely impaired binding affinity for folate and 5-formyl-tetrahydrofolate (FTHF) and a corresponding defect in its folate-dependent enzyme activity
malfunction
serine hydroxymethyltransferase 2 (SHMT2) protein is overexpressed at the protein level in an amplicon-positive rhabdomyosarcoma (RMS) cell line, SHMT2 contributes to tumorigenesis in fusion-positive (FP) RMS. SHMT2 knockdown in amplicon-positive RMS cells suppresses growth, transformation, and tumorigenesis, whereas overexpression in amplicon-negative RMS cells promots these phenotypes. High SHMT2 expression reduces sensitivity of FP RMS cells to SHIN1, a direct SHMT2 inhibitor, but sensitized cells to pemetrexed, an inhibitor of the folate cycle
malfunction
overexpression of SHMT2 in human cancer cells leads to increased serine catabolism which supports malignant growth through diverse mechanisms, including enhanced nucleotide synthesis, redox balance, mitochondrial translation, DNA and histone methylation, and suppression of retrotransposon activa. Increased SHMT2 expression triggers follicular lyphoma development in vivo, overview. Targeting SHMT2 expression or activity shows antilymphoma activity that is enhanced by concurrent BCL2 inhibition
malfunction
increased SHMT2 expression triggers follicular lyphoma development in vivo, overview. Shmt2 knockdown reduces lymphomagenesis driven by MYC in the context of VavP-Bcl2 transgenic hematopoietic stem cells (HSCs) leading to significantly increased survival. Targeting SHMT2 expression or activity shows antilymphoma activity that is enhanced by concurrent BCL2 inhibition
malfunction
-
mutation of SHMT1 clearly exhibit chlorotic and lethal phenotypes under ambient growth conditions, which are rescued by elevated CO2 and partially by GSH. Mutant shm1-2 exhibits a severe root-retardation phenotype at low-sucrose conditions with increased H2O2 levels, and plants with SHMT1 overexpression have longer roots with reduced H2O2 levels. Sugar-feeding assays, ROS scavenging by GSH, or reduction of RBOHD expression partially restore the root-growth inhibition phenotype at low-sucrose conditions. Exogenous sucrose rescued the root-growth-arrest phenotype of shm1-2 mutant, but elevated CO2 alone does not, overview
-
malfunction
-
mutant DELTAshmT is susceptible to the lysostaphin, while complementation of the knockout expressing shmT restores resistance against lysostaphin. In addition, the DELTAshmT shows reduced virulence under in vitro (mammalian cell lines infection) and in vivo (wax-worm infection) models. The SHMT inhibitor, serine hydroxymethyltransferase inhibitor 1 (SHIN1), protects the 50% of the wax-worm infected with wild type Staphylococcus aureus
-
malfunction
Aedes aegypti NIH Rockefeller
-
digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal
-
malfunction
Glycine max F650
-
the P285S substitution decreases stability of the SHMT8 tetramer, increases protein flexibility and reduces thermal stability
-
metabolism
-
SHMT1 is a rate-limiting enzyme in de novo thymidylate biosynthesis
metabolism
-
the enzyme regulates the partitioning of 5,10-methylenetetrahydrofolate between the thymidylate and homocysteine remethylation pathways, mitochondrial SHMT-derived one-carbon units are essential for folate-mediated one-carbon metabolism in the cytoplasm
metabolism
-
the de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation, SHMT1 scaffold function can determine de novo thymidylate synthesis capacity, SHMT1 interaction with TYMS and DHFR is DNA-dependent, but the formation of thymidylate biosynthesis complex is nucleotide-independent. Folate-mediated one-carbon metabolism in the cytoplasm and nucleus, overview
metabolism
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes
metabolism
the enzyme plays an essential role in one-carbon unit metabolism
metabolism
the enzyme is involved in folate recycling and dTMP synthesis
metabolism
key role for serine and glycine metabolism in the survival of brain cancer cells within the ischemic zones of gliomas. Glycine decarboxylase inhibition impairs cells with high SHMT2 levels as the excess glycine not metabolized by glycine decarboxylase can be converted to the toxic molecules aminoacetone and methylglyoxal. SHMT2 activity limits that of pyruvate kinase (PKM2) and reduces oxygen consumption, eliciting a metabolic state that confers a profound survival advantage to cells in poorly vascularized tumor regions
metabolism
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the mitochondrial isoform SHMT2 is a crucial factor in the serine/glycine metabolism in several cancer cell types. Correlation of expression level of SHMT2 and other clinicopathological parameters in clinical breast cancer, overview
metabolism
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Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
metabolism
the enzyme is involved in the one-carbon metabolism, which provides one-carbon units for the biosynthesis of nucleotides, methylation reactions and redox homeostasis
metabolism
serine hydroxymethyltransferase (SHMT) is engaged in glycine biosynthesis from serine. The threonine-cleavage activity of the Ta0811 protein, glycine hydroxymethyltransferase related protein in Thermoplasma acidophilum, is 3.5 times higher than the serine-cleavage activity of Ta1509 protein. The serine hydroxymethyltransferase seems to play a minor role in glycine biosynthesis in Thermoplasma acidophilum
metabolism
SHMT is indispensable for the one-carbon metabolism of serine/glycine interconversion and is linked to folate metabolism
metabolism
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the serine hydroxymethyltransferase participates in glycine-serine interconversion of one-carbon metabolism in the sulfur assimilation pathway. Cysteine-rich proteins play an important role in the formation of protein bodies in rice
metabolism
serine hydroxymethyltransferase (SHMT) is one of the key enzymes of the one-carbon metabolic pathway
metabolism
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance
metabolism
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance
metabolism
SHMT2 acts as an important enzyme in one-carbon unit metabolism pathway. In mitochondria, SHMT2-dependent production of methylene-THF contributes to mitochondrial NADPH generation and redox balance during hypoxia. SHMT2 is a transcriptional target of Myc, illustrating an intrinsic link between tumorigenesis and cellular metabolism. SHMT2 can activate the Akt/mTOR signaling pathway by its metabolic product, which facilitates hepatocyte cell regeneration
metabolism
SHMT2 changes the epigenetic control of gene expression. MYC regulates the expression of SHMT2 in human transformed follicular lymphoma (tFL)
metabolism
OsSHMT interacts with ATP synthase subunit alpha, heat shock protein Hsp70, mitochondrial substrate carrier family protein, ascorbate peroxidase 1 and ATP synthase subunit beta
metabolism
SHMT2 changes the epigenetic control of gene expression. MYC regulates the expression of SHMT2 in mice transformed follicular lymphoma (tFL)
metabolism
the enzyme is involved in the 1C metabolic pathway, overview. The 1C metabolism is important for the biosynthesis of metabolites necessary for cellular replication
metabolism
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the enzyme plays an essential role in one-carbon unit metabolism
-
metabolism
-
Shm2 is a key enzyme at the crossing point between purine, methionine and folate metabolism
-
metabolism
-
serine hydroxymethyltransferase (SHMT) is engaged in glycine biosynthesis from serine. The threonine-cleavage activity of the Ta0811 protein, glycine hydroxymethyltransferase related protein in Thermoplasma acidophilum, is 3.5 times higher than the serine-cleavage activity of Ta1509 protein. The serine hydroxymethyltransferase seems to play a minor role in glycine biosynthesis in Thermoplasma acidophilum
-
metabolism
-
serine hydroxymethyltransferase (SHMT) is engaged in glycine biosynthesis from serine. The threonine-cleavage activity of the Ta0811 protein, glycine hydroxymethyltransferase related protein in Thermoplasma acidophilum, is 3.5 times higher than the serine-cleavage activity of Ta1509 protein. The serine hydroxymethyltransferase seems to play a minor role in glycine biosynthesis in Thermoplasma acidophilum
-
metabolism
-
SHMT is indispensable for the one-carbon metabolism of serine/glycine interconversion and is linked to folate metabolism
-
metabolism
-
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance
-
metabolism
-
serine hydroxymethyltransferase (SHMT) is engaged in glycine biosynthesis from serine. The threonine-cleavage activity of the Ta0811 protein, glycine hydroxymethyltransferase related protein in Thermoplasma acidophilum, is 3.5 times higher than the serine-cleavage activity of Ta1509 protein. The serine hydroxymethyltransferase seems to play a minor role in glycine biosynthesis in Thermoplasma acidophilum
-
metabolism
-
serine hydroxymethyltransferase (SHMT) is engaged in glycine biosynthesis from serine. The threonine-cleavage activity of the Ta0811 protein, glycine hydroxymethyltransferase related protein in Thermoplasma acidophilum, is 3.5 times higher than the serine-cleavage activity of Ta1509 protein. The serine hydroxymethyltransferase seems to play a minor role in glycine biosynthesis in Thermoplasma acidophilum
-
physiological function
-
the UV-induced increase in SHMT1 translation is accompanied by an increase in the small ubiquitin-like modifier-dependent nuclear localization of the de novo thymidylate biosynthesis pathway and a decrease in DNA strand breaks, suggesting that SHMT1 plays a role in DNA repair
physiological function
-
cytoplasmic serine hydroxymethyltransferase regulates the metabolic partitioning of methylenetetrahydrofolate but is not essential in mice
physiological function
-
the mitochondrial SHMT is required for photorespiration
physiological function
salt-induced ApSHMT increases the level of glycine betaine via L-serine and choline and confers tolerance to salinity stress
physiological function
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functional redundancy of SHMT2alpha and SHMT1 in nuclear de novo thymidylate synthesis. The de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation. SHMT expression is rate-limiting for de novo thymidylate synthesis
physiological function
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serine hydroxymethyltransferases are important enzymes of cellular one-carbon metabolism and are essential for the photorespiratory glycine-into-serine conversion in leaf mesophyll mitochondria. SHM1 is the photorespiratory isozyme. Due to exclusion of SHM2 from the photorespiratory environment of mesophyll mitochondria, SHM2 cannot substitute for SHM1 in photorespiratory metabolism. SHM1 and SHM2 operate in a redundant manner in one-carbon metabolism of nonphotorespiring cells with a high demand of one-carbon units, e.g. during lignification of vascular cells, detailed overview
physiological function
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the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate,which serves as a storage formof reduced folates and onecarbon groups in cells in a dormant stage
physiological function
-
the reaction catalyzed by this enzyme, the reversible transfer of the Cbeta of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes, e.g. as a primary source of the one carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the hydrolysis of 5,10-methenyl-tetrahydropteroylglutamate to 5-formyl-tetrahydropteroylglutamate, which serves as a storage form of reduced folates and one-carbon groups in cells in a dormant stage
physiological function
-
the enzyme is essential for the acquisition of one-carbon units for subsequent transfer reactions
physiological function
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism
physiological function
-
the enzyme is essential for parasite viability
physiological function
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the enzyme is crucial for deoxythymidylate biosynthesis and a target for antimalarial drug development, the Plasmodium vivax enzyme catalyzes the reaction via a ternary complex mechanism
physiological function
mitochondrial serine hydroxymethyltransferase seems to be fundamental to sustain cancer metabolism since production of glycine fuels heme biosynthesis and therefore oxidative phosphorylation. Respiration of cancer cells may then ultimately rely on endogenous glycine synthesis by mitochondrial serine hydroxymethyltransferase. The link between mitochondrial serine hydroxymethyltransferase activity and heme biosynthesis represents an important aspect of cancer cell metabolism. Glycine itself, rather than one-carbon units deriving from the SHMT2 reaction, is specifically critical in cancer cells
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the 5,10-methylenetetrahydropteroylglutamate-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMT2 is required for cancer cells to adapt to the tumor environment, but also renders these cells sensitive to glycine cleavage system inhibition. The enzyme has a key role in cells in environments with limited oxygen or nutrient levels
physiological function
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SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
A0A069BAT4
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
physiological function
the enzyme dynamically changes the fluxes of one-carbon metabolism by reversibly converting L-serine and tetrahydrofolate into 5,10-methylene-tetrahydrofolate and glycine. The cytosolic isoforms can also translocate to the nucleus to sustain de novo thymidylate synthesis and support cell proliferation
physiological function
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the enzyme has additional functions aside from its main enzymatic role in soybean cyst nematode resistance
physiological function
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Synechococcus elongatus PCC7942 cells expressing the enzyme from Aphanothece halophytica reveal an increase in growth under salt stress condition
physiological function
cytosolic serine hydroxymethyltransferase controls lung adenocarcinoma cells migratory ability by modulating AMP kinase activity. The level of the amino acid serine in the cytosol affects the migratory properties of lung adenocarcinoma (LUAD) cells. Cytosolic serine levels controlled by SHMT1 modulate ROS formation and ATP/energy profile. Addition of serine in the growth medium significantly increases both respiration and glycolysis. AMP kinase is the sensor of serine starvation modulating cell migration. Preferential migration of LUAD cells in the brain
physiological function
cytosolic serine levels controlled by SHMT1 modulate ROS formation and ATP/energy profile. The metabolism of specific amino acids, i.e., serine and glycine, found in the brain microenvironment, plays an active role in the control of adenocarcinoma cell motility. The uptake of extracellular serine and glycine is required for migration, and motility of cancer cells can be effectively impaired by using inhibitors of the serine/glycine transporters SLC1A4/SLC1A5 and GlyT1, which are involved in this process. Preferential migration of lung adenocarcinoma (LUAD) cells in the brain
physiological function
serine hydroxymethyl transferase (Shmt) is required for proper brain development affecting primarily optic lobe development. Shmt has a role in cellular growth and proliferation and is required for optic lobe neuroepithelia development in Drosophila melanogaster
physiological function
Ta1509 protein exhibits dual activities to catalyze tetrahydrofolate (THF)-dependent serine cleavage and THF-independent threonine cleavage, cf. EC 4.1.2.48
physiological function
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
physiological function
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
physiological function
serine hydroxymethyltransferase (SHMT) is indispensable for the one-carbon metabolism of serine/glycine interconversion and is linked to folate metabolism. SHMT plays a key role in lysostaphin resistance development and in determining the virulence potential of multiple drug-resistant Staphylococcus aureus. Lysostaphin resistance pattern in ST72 isolates, overview. The shmT gene contributes to the survival of strain USA300 inside the host cells, and possibly plays an important role in the virulence and pathogenesis
physiological function
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gene LCRP encodes a serine hydroxymethyltransferase, which participates in glycine-serine interconversion of one-carbon metabolism in the sulfur assimilation pathway. The serine hydroxymethyltransferase participates in the synthesis of cysteine-rich storage proteins in rice seed
physiological function
the enzyme serine hydroxymethyltransferase (SHMT) plays a key role in folate metabolism and is conserved in all kingdoms of life. SHMT is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of L-serine and (6S)-tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate
physiological function
ITBSHMT_1 is able to synthesize various beta-hydroxy amino acids such as serine, threonine, and phenylserine
physiological function
mitochondrial serine hydroxymethyltransferase 2 (SHMT2) is an important drug target in the one-carbon metabolic pathway, since its activity is critical for purine and pyrimidine biosynthesis. SHMT2 plays a prominent role during metabolic reprogramming of cancer cells
physiological function
serine hydroxymethyltransferase (SHMT2) is one of the key enzymes associated with serine and folate metabolism and represents the mitochondrial form of a pyridoxal phosphate-dependent enzyme that catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate, an essential intermediate for the biosynthesis of purines, thymidine and methionine. Serine hydroxymethyltransferase (SHMT2) plays a multifunctional role in mitochondria. The expression of the SHMT2 gene is controlled by ERN1 protein kinase and induced by hypoxia as well as glutamine and glucose deprivation conditions in glioblastoma cells reflecting the reprogramming of sensitivity of this gene expression to nutrient deprivation mediated by ERN1, an endoplasmic reticulum transmembrane signaling protein with protein kinase and endoribonuclease activities in the cytoplasmic domain
physiological function
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance, as in the case of SHMT from the halophilic cyanobacterium Aphanothece halophytica (AhSHMT). The catalytic activity of SHMT2 itself plays a fundamental role in salt tolerance
physiological function
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance, as in the case of SHMT from the halophilic cyanobacterium Aphanothece halophytica (AhSHMT). The catalytic activity of SHMT2 itself plays a fundamental role in salt tolerance
physiological function
gene SHMT1 encodes a key enzyme in the photorespiration process, which catalyzes the conversion of glycine into serine. SHMT1 is also reported to participate in biotic or abiotic stress responses. Serine hydroxymethyltransferase 1 (SHMT1) is essential for primary-root growth at low-sucrose conditions via linking the sucrose with the redox state in Arabidopsis thaliana, overview. Accumulation of H2O2 in the primary roots is altered by SHMT1 expression changes at low-sucrose conditions
physiological function
SHMT2 amplification predicts differential response to drugs targeting the metabolic pathway
physiological function
SHMT2 is primarily involved in the production of glycine and 5,10-CH2-THF. In a variety of human tumours, including hepatocellular carcinoma (HCC), breast cancer and non-small cell lung cancer (NSCLC), a large amount of carbon is reused in serine/glycine biosynthesis, accompanied by higher expression of the key glycine synthetic enzyme mitochondrial serine hydroxymethyltransferase 2 (SHMT2). This enzyme can convert serine into glycine and a tetrahydrofolate-bound one-carbon unit, ultimately supporting thymidine synthesis and purine synthesis and promoting tumour growth. In tumour samples, elevated expression of SHMT2 is associated with poor prognosis. Roles of mitochondrial serine hydroxymethyltransferase 2 (SHMT2) in human carcinogenesis and SHMT2 deregulation in human cancers, detailed overview. SHMT2 as a candidate oncogenic driver gene across multiple solid tumour types. Upon treatment with IFNalpha, fatty-acylated SHMT2 is recruited to late endosomes/lysosomes to deubiquitinate IFNalphaR1 and activate IFN signaling
physiological function
serine hydroxymethyltransferase-2 (SHMT2) is a key mitochondrial enzyme in serine catabolism that converts serine to glycine and a one-carbon unit that yields S-adenosyl methionine (SAM) and NADPH through the folate and methionine cycles. Role of the enzyme serine hydroxymethyltransferase-2 (SHMT2) in lymphoma initiation. SHMT2 is an oncogenic driver of BCL2-expressing lymphomas and acts, at least in part, through silencing of previously uncharacterized tumor suppressor genes. SHMT2 contributes to the biology of aggressive human lymphomas. SHMT2 changes the epigenetic control of gene expression, overview
physiological function
serine hydroxymethyltransferase plays a role in scavenging H2O2 to enhance rice chilling tolerance, regulation network of OsSHMT in rice under chilling stress
physiological function
wild-type SHMT2 enzyme acts as an oncogenic trigger in a Bcl2 transgenic mouse model of follicular lymphoma. SHMT2 contributes to the biology of aggressive murine lymphomas. SHMT2 changes the epigenetic control of gene expression, overview
physiological function
serine hydroxymethyltransferase (SHMT) plays a critical role in the 1C metabolism pathway. This pathway is involved in the synthesis of many amino and nucleic acids, and SHMT is considered a target for drugs through folate metabolism, especially for cancer and malaria
physiological function
serine hydroxymethyltransferase (SHMT) 2 is a pyridoxal 5'-phosphate (PLP)-associated enzyme that catalyzes the conversion of serine to glycine in mitochondria, resulting in generation of 5,10-methylene tetrahydrofolate (mTHF) from THF
physiological function
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SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
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physiological function
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gene SHMT1 encodes a key enzyme in the photorespiration process, which catalyzes the conversion of glycine into serine. SHMT1 is also reported to participate in biotic or abiotic stress responses. Serine hydroxymethyltransferase 1 (SHMT1) is essential for primary-root growth at low-sucrose conditions via linking the sucrose with the redox state in Arabidopsis thaliana, overview. Accumulation of H2O2 in the primary roots is altered by SHMT1 expression changes at low-sucrose conditions
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
Lathyrus oleraceus Progress 9
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in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
-
physiological function
-
in plastids, SHMTs are thought to catalytically direct the hydroxymethyl moiety of serine into the metabolic network of H4PteGlun-bound one-carbon units
-
physiological function
-
Ta1509 protein exhibits dual activities to catalyze tetrahydrofolate (THF)-dependent serine cleavage and THF-independent threonine cleavage, cf. EC 4.1.2.48
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physiological function
-
Ta1509 protein exhibits dual activities to catalyze tetrahydrofolate (THF)-dependent serine cleavage and THF-independent threonine cleavage, cf. EC 4.1.2.48
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
-
physiological function
-
SHMT plays an important role in the assimilation of C1 compounds, yielding the main L-serine intermediate
-
physiological function
-
serine hydroxymethyltransferase (SHMT) is indispensable for the one-carbon metabolism of serine/glycine interconversion and is linked to folate metabolism. SHMT plays a key role in lysostaphin resistance development and in determining the virulence potential of multiple drug-resistant Staphylococcus aureus. Lysostaphin resistance pattern in ST72 isolates, overview. The shmT gene contributes to the survival of strain USA300 inside the host cells, and possibly plays an important role in the virulence and pathogenesis
-
physiological function
-
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
-
physiological function
-
serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate-dependent enzyme that plays a pivotal role in cellular one-carbon metabolism. In plants and cyanobacteria, this enzyme is also involved in photorespiration and confers salt tolerance, as in the case of SHMT from the halophilic cyanobacterium Aphanothece halophytica (AhSHMT). The catalytic activity of SHMT2 itself plays a fundamental role in salt tolerance
-
physiological function
-
Ta1509 protein exhibits dual activities to catalyze tetrahydrofolate (THF)-dependent serine cleavage and THF-independent threonine cleavage, cf. EC 4.1.2.48
-
physiological function
-
Ta1509 protein exhibits dual activities to catalyze tetrahydrofolate (THF)-dependent serine cleavage and THF-independent threonine cleavage, cf. EC 4.1.2.48
-
physiological function
Mus musculus B6EiC3SnF1/J
-
cytosolic serine levels controlled by SHMT1 modulate ROS formation and ATP/energy profile. The metabolism of specific amino acids, i.e., serine and glycine, found in the brain microenvironment, plays an active role in the control of adenocarcinoma cell motility. The uptake of extracellular serine and glycine is required for migration, and motility of cancer cells can be effectively impaired by using inhibitors of the serine/glycine transporters SLC1A4/SLC1A5 and GlyT1, which are involved in this process. Preferential migration of lung adenocarcinoma (LUAD) cells in the brain
-
physiological function
Psychromonas ingrahamii DSM 17664
-
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
-
physiological function
Psychromonas ingrahamii CCUG 51855
-
using PLP as the cofactor, SHMT carries out interconversion of serine and glycine by catalyzing the reversible transfer of C of serine to tetrahydropteroylglutamate (H4PteGlu), resulting in the formation of glycine and 5,10-methylene-H4PteGlu. This reaction provides a primary source of one-carbon units required for the synthesis of thymidylate, purines, and methionine. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and decarboxylation of aminomalonate, which is similar to H4PteGlu-dependent serine cleavage. Because of the observed increased activity of SHMT in neoplastic tissues and its essential role in nucleotide biosynthesis, SHMT has been suggested as a potential target for cancer therapy
-
physiological function
Glycine max F650
-
the enzyme serine hydroxymethyltransferase (SHMT) plays a key role in folate metabolism and is conserved in all kingdoms of life. SHMT is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of L-serine and (6S)-tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate
-
physiological function
-
ITBSHMT_1 is able to synthesize various beta-hydroxy amino acids such as serine, threonine, and phenylserine
-
additional information
amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
-
amino acid residues important for the structure and function of SHMT are Y56, D202, and K231 for the interaction with pyridoxal 5'-phosphate, R64 and D73 for inter-subunit interaction, H127 for cofactor binding, and P258 and R363 for substrate interaction
additional information
-
kinetic properties of SHM2 might render this enzyme unsuitable for the high-folate conditions of photorespiring mesophyll mitochondria
additional information
-
both PfSHMTc and PfSHMTm show dynamic, stage-dependent localization among the different compartments of the parasite and sequence analysis suggests they may also reversibly associate with each other, a factor that may be critical to folate cofactor function, given the apparent lack of enzymic activity of PfSHMTm
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
additional information
the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
-
the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1DFO, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1KKJ, molecular dynamics, overview
additional information
A0A069BAT4
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3GBX, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4N0W, molecular dynamics, overview
additional information
three-dimensional enzyme structure analysis using crystal structure with PDB ID 1DFO, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
additional information
three-dimensional enzyme structure analysis using crystal structure with PDB ID 4P3M, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
additional information
treatment with 2 U of lysostaphin eradicates most of the Staphylococcus aureus ST72 isolates and strain USA300. However, the ST72 isolates from human K07-204, animal 08-B-93, and soil 4-009 isolates show differential resistance to lysostaphin. Role of shmT in lysostaphin resistance, mechanism, overview
additional information
like other PLP-dependent enzymes, SHMT also undergoes the so-called transimination reaction before exhibiting its enzymatic activity, free energy landscape and proton transfer pathways of the transimination reaction at the active site of the serine hydroxymethyltransferase enzyme in aqueous medium, investigated by employing hybrid quantum mechanical/molecular mechanical (QM/MM) simulations combined with metadynamics methods of rare event sampling, docking analysis, overview
additional information
the enzyme has a single conserved cis proline, P285, which is located near the active site. Pro285 is adjacent to both the PLP and THF-binding sites of the enzyme. Pro285 also participates in the sole cis-peptide bond in the polypeptide chain of SHMT8 (471 amino acids). Isozyme SHMT8 structure comparisons, overview
additional information
ITBSHMT_1 has 5 additional residues VSRQG on loop near PLP-binding site as structural feature which distinguish this enzyme with other characterized SHMTs. Docking and binding analysis using tetrahydrofolate (THF), 5-formyl-tetrahydrofolate/5-formyltetrahydropteroylglutamate (FFO), and pyridoxal 5'-phosphate-glycine (PLG), overview
additional information
the kinetic properties of AhSHMT correlate with those of the mesophilic orthologue from Escherichia coli, but AhSHMT appears more catalytically efficient, especially in presence of salt. Possible role of specific amino acid residues implicated in the halophilic features of AhSHMT, structure analysis, overview
additional information
the kinetic properties of the enzyme from cyanobacterium Aphanothece halophytica (AhSHMT) correlate with those of the mesophilic orthologue eSHMT from Escherichia coli, but AhSHMT appears more catalytically efficient, especially in presence of salt. Possible role of specific amino acid residues implicated in the halophilic features of AhSHMT, structure comparisons, overview
additional information
Psychrobacter sp. ANT206
A0A7L7SZS9
enzyme PsSHMT three-dimensional structure homology modeling, PsSHMT owns fewer proline residues and hydrogen bonds compared with its homologues from mesophilic Escherichia coli and thermophilic Geobacillus stearothermophilus, overview. PsSHMT possesses Gly-PLP binding sites (Ser34, Tyr54, Tyr64, Gly97, Ser98, His125, Ser175, Asp200, His203, His228, Lys229, Arg235, and Arg361) and conserved folate binding sites (Glu56, Tyr63, Leu120, Gly124, Leu126, Phe255, and Asn345). And the active sites of PsSHMT are identified to be Ser34, His125, Lys229, and Arg361. The Lys residues might not be an essential group of the active center of the activity of rPsSHMT
additional information
SHMT2 localizes to the most frequent region of copy number gains at chromosome 12q14.1 in lymphoma. SHMT2 is a target of the chromosome 12q14.1 amplicon in a large fraction of human B-cell lymphomas
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview
-
additional information
-
three-dimensional enzyme structure analysis using crystal structure with PDB ID 4P3M, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview
-
additional information
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview
-
additional information
-
treatment with 2 U of lysostaphin eradicates most of the Staphylococcus aureus ST72 isolates and strain USA300. However, the ST72 isolates from human K07-204, animal 08-B-93, and soil 4-009 isolates show differential resistance to lysostaphin. Role of shmT in lysostaphin resistance, mechanism, overview
-
additional information
-
three-dimensional enzyme structure analysis using crystal structure with PDB ID 1DFO, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
-
the kinetic properties of the enzyme from cyanobacterium Aphanothece halophytica (AhSHMT) correlate with those of the mesophilic orthologue eSHMT from Escherichia coli, but AhSHMT appears more catalytically efficient, especially in presence of salt. Possible role of specific amino acid residues implicated in the halophilic features of AhSHMT, structure comparisons, overview
-
additional information
Psychromonas ingrahamii DSM 17664
-
three-dimensional enzyme structure analysis using crystal structure with PDB ID 4P3M, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
Psychromonas ingrahamii CCUG 51855
-
three-dimensional enzyme structure analysis using crystal structure with PDB ID 4P3M, structure-activity analysis and flexibility mechanism, overview. When compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
Glycine max F650
-
the enzyme has a single conserved cis proline, P285, which is located near the active site. Pro285 is adjacent to both the PLP and THF-binding sites of the enzyme. Pro285 also participates in the sole cis-peptide bond in the polypeptide chain of SHMT8 (471 amino acids). Isozyme SHMT8 structure comparisons, overview
-
additional information
-
ITBSHMT_1 has 5 additional residues VSRQG on loop near PLP-binding site as structural feature which distinguish this enzyme with other characterized SHMTs. Docking and binding analysis using tetrahydrofolate (THF), 5-formyl-tetrahydrofolate/5-formyltetrahydropteroylglutamate (FFO), and pyridoxal 5'-phosphate-glycine (PLG), overview
-
Show AA Sequence and Transmembrane Helices (33850 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000 - 200000
200000
200000 - 204000
-
mitochondria, gel filtration, PAGE, amino acid composition
210000
215000
216000
220000
230000
25000
-
refolded pyridoxal-5'-phosphate-binding domain of SHMT, gel filtration
44500
x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
45000
45050
2 * 45050, recombinant N-terminally His-tagged enzyme, mass spectrometry
50000
52020
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
53000
54000
55000
60000
x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
90000
91000
98000
additional information
180000 - 200000
-
gel filtration, sucrose density gradient centrifugation
53000
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
91000
wild type SHMT exists as a dimer in both apo- and holo-forms, ultracentrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
the apo-L276A and the apo-L85A mutants are in the monomeric state
tetramer
additional information
?
x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
?
-
x * 44500, about, sequence calculation, x * 60000, recombinant GST-tagged enzyme, SDS-PAGE
-
dimer
-
homology modeling and comparison to SHMT from Bacillus stearothermophilus, using the crystal structure, PDB ID 1KKJ, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
A0A069BAT4
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
in the 0.0025-0.025 mM subunit concentration range, the wild type SHMT is a dimer, either in the presence or absence of cofactor. The apo-L85A mutant enzyme is approximately 75% dimeric
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
homology modeling using the crystal structure, PDB ID 1KKJ, and comparison to SHMT from Bacillus subtilis, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
-
removal of the bound pyridoxal 5'-phosphate from the mutant tetrameric enzyme leads to dissociation to a dimer
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
2 * 45050, recombinant N-terminally His-tagged enzyme, mass spectrometry
dimer
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
-
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
-
dimer
Psychromonas ingrahamii CCUG 51855
-
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
-
dimer
Psychromonas ingrahamii DSM 17664
-
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
-
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
dimer
-
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
-
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
homodimer
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
homodimer
-
three-dimensional enzyme three-domain structure analysis using crystal structure with PDB ID 1DFO, overview. The functional dimer contains two active sites, each in one monomer. Of note is that the entrances of both active-site cavities are located at the inter-monomer interfaces, and some of the residues participating in the formation of the active site in one monomer come from the other monomer
-
homotetramer
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE
tetramer
crystal structure analysis of wild-type and mutant enzymes, overview
tetramer
-
4 * 53000, wild-type enzyme and mutant enzymes C203F and W110F, SDS-PAGE
additional information
-
the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in typr I fold enzymes, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
additional information
-
the folding mechanism of SHMT is divided in two phases and terminates with pyridoxal 5'-phosphate binding. In the first one, the large and small domains rapidly assume their native state, forming a folding intermediate that is not able to bind pyridoxal 5'-phosphate. In the second, slower phase, the enzyme folds into the native structure, acquiring the capability to bind the cofactor. Importance of the third hydrophobic cluster, highly conserved in type I fold enzyme, as key structural determinant of the assembly of eSHMT active site and overall native fold. This cluster plays a fundamental role in the transition from the first to the second phase of SHMT folding process
additional information
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
additional information
-
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
-
90% dimer and 10% tetramer in the same organism, one subunit: 45000 Da, SDS-PAGE
additional information
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
additional information
-
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
Psychromonas ingrahamii CCUG 51855
-
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
additional information
Psychromonas ingrahamii DSM 17664
-
when compared to the warm-active mesophilic mSHMT from Escherichia coli, the cold-adapted psychrophilic pSHMT from Psychromonas ingrahamii experiences not only more drastic conformational fluctuations at both the levels of the entire dimer and individual monomers, but also larger relative monomer movements. Thus, pSHMT has a lower structural stability and a stronger capability to change conformation than mSHMT
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
SHMT2 can be acetylated at lysine K95 in different cancer cells, including CRC cells. K95 acetylation inhibits SHMT2 enzymatic activity and promotes its degradation via macroautophagy. SIRT3, a deacetylase localized in the mitochondria, deacetylates SHMT2 and eventually increases its activity to promote cell proliferation and colorectal carcinogenesis
lipoprotein
HDAC11 has been proven to be an efficient lysine defatty-acylase that directly removes fatty acyl groups from SHMT2. MCF-7 and A549 cells, knockdown of HDAC11 significantly increases the fatty acylation level of SHMT2. Although SHMT2 fatty acylation does not affect its enzymatic activity, K245 is the major fatty acylation site of HDAC11. Upon treatment with IFNalpha, fatty-acylated SHMT2 is recruited to late endosomes/lysosomes to deubiquitinate IFNalphaR1 and activate IFN signaling
side-chain modification
succinylation
SHMT2 interacts with nicotinamide adenine dinucleotide (NAD+)-dependent lysine desuccinylase SIRT5 directly. Under metabolic stress, desuccinylation at lysine 280 of SHMT2 by SIRT5 enhances SHMT2 activity to accelerate cell metabolism and facilitate cell proliferation and tumour growth in vivo and in vitro
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
side-chain modification
-
in addition to the lysine residue involved in Schiff base formation with the PLP, other residues like arginine, histidine, cysteine and tryptophan essential for catalysis, review
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His-tagged enzyme AhSHMT in three forms, as internal aldimine, as external aldimine with the L-serine substrate, and as a covalent complex with malonate, hanging drop vapor diffusion method, mixing of protein in 20 mM potassium phosphate, pH 7.2, 300 mM NaCl, and 1 mM PLP, with 0.2 M sodium malonate, pH 5.0, and 20% PEG 3350 for the malonate complex, or with 0.05 M citric acid, 0.05 M Bis-Tris propane, pH 5.0, and 16% PEG 3350 for the internal aldimine state enzyme, or with 0.2 M sodium malonate, pH 5.0, and 20% PEG 3350, and 50 mM L-serine for the external aldimine state enzyme, X-ray diffraction structure determination and analysis at 1.25-1.77 A resolution, molecular replacement using the structure of SHMT from Geobacillus stearothermophilus as a search probe (PDB ID 1kkj)
purified recombinant detagged enzyme in complex with inhibitor mangiferin, sitting-drop vapor diffusion, 20°C, mixing of 800 nl of protein solution and 800 nl of reservoir solution, the latter contains 0.01 M MgCl2, 0.05 M MES, pH 5.8, 1.9 M Li2SO4, and 2 mM mangiferin, X-ray diffraction structure determination and analysis at 2.25 A resolution
crystals of K226M and K226Q mutant enzymes and of the complex of mutant enzyme K226Q with Gly or mutant enzyme K226M with Ser. Crystals are obtained by mixing 0.004 ml of protein solution 0.375 mM with 0.004 mM of reservoir solution containing 100 mM Hepes buffer, pH 7.5, 0.2 mM EDTA, 5 mM 2-mercaptoethanol, and 50% 2-methyl-2,4-pentanediol
-
crystals of Y51F and Y61A SHMT mutants are obtained by hanging drop vapour diffusion using 50% (v/v) 2-methyl 2,4-pentanediol as the precipitant
-
internal aldimine form, external aldimine form with bound serine and glycine, ternary complex with glycine and 5-formyl tetrahydrofolate
-
mutant proteins are crystallized by the hanging drop vapor diffusion method, using 50% 2-methyl 2,4-pentanediol as the precipitant with 0.2 mM EDTA, 5 mM beta-mercaptoethanol in 100 mM HEPES (pH 7.5)
determination of five crystal structures of the 1884-residue SHMT8 tetramers from the SCN-susceptible cv. Essex and the SCN-resistant cv. Forrest. Crystallization of purified recombinant enzymes, sitting drop vapor diffusion method, mixing of 12 mg/ml protein in 25mM HEPES, pH 7.5, 50 mM NaCl, and 0.5 mM TCEP, with reservoir solution, containing 0.2 M trimethylamine N-oxide hydrate, 0.1 M Tris, pH 8.5, 20% w/v PEG monomethyl ether 2000, a 1:1 protein:reservoir ratio, followed by crystals seeding into 0.175-0.24 M trimethylamine N-oxide hydrate, 0.1 M Tris, pH 8.5, and 19-23 w/v PEG monomethyl ether 2000. For the structure of Essex SHMT8 complexed with PLP-Gly, the crystals are 20 mM glycine in both the protein sample and the reservoir solution is added. For the structure of Forrest SHMT8 complexed with PLP-Gly, crystals are obtained by soaking Forrest SHMT8-PLP crystals in reservoir solution supplemented with 20 mM L-serine and 15% v/v ethylene glycol for cryoprotection, X-ray diffraction structure determination and analysis at 1.4-2.35 A resolution, molecular replacement using the structure of rabbit SHMT (PDB ID 1CJ0) as a template structure, and modelling
purified recombinant tetrameric enzyme mutant P285S free or in complex with PLP and PLP-glycine external aldimine intermediate, sitting drop vapor diffusion method, mixing of 0.002 ml of 12 mg/ml protein in 50 mM HEPES, 150 mM NaCl, 0.5 mM TCEP, and 0.12 mM PLP with 0.002 ml of reservoir solution containing 2% v/v Tacsimate, pH 7.0, 0.1 M HEPES, pH 7.5, and 20% w/v PEG 3350, equilibration against 0.1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution, molecular replacement using implementation of the Essex SHMT8-PLP co-ordinates (PDB ID 6UXH), modelling
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M sodium acetate
holo- and apo-isoform SHMT2, hanging drop vapor diffusion method, using 0.1 M Bis/Tris propane pH 7.5, 5% (v/v) glycerol, 12-16% (w/v) poly(ethylene glycol) 3350, 0.2 M potassium fluoride
mutant H135N/R137A/E168N, hanging drop vapor diffusion method, using 0.1 M sodium cacodylate pH 6.5, 1.0 M sodium citrate
purified PLP-bound truncated enzyme His-SHMT2DELTAN30, wild-type sequence and Y105A, Y105F, Y106A, or Y106F mutants, in complex with antifolates AGF320 and AGF347, X-ray diffraction structure determination and analysis, structure modelling
sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 28% (w/v) PEGMME 2000 (in complex with lometrexol and methotrexate), 0.2 M LiCl2, 0.1 M MES pH 6.0, 20% (w/v) PEG6000 (in complex with pemetrexed), and 0.2 M NaCl, 0.1 M MES pH 6.0, 20% (w/v) PEG6000 (in complex with raltitrexed)
hanging drop vapor diffusion method, using 18% (w/v) PEG 8000, 0.1 M MES pH 6.0, 0.2 M Ca(OAc)2
apoenzyme,hanging drop vapor diffusion method, using 55% tacsimate pH 7.0. Enzyme bound to reaction intermediates, hanging drop vapor diffusion method, using 75 mM MES pH 6.5, 19%(w/v) polyethylene glycol 3350 and 150 mMammonium acetate
crystal structure of the apoenzyme and pyridoxal 5'-phosphate-bound holoenzyme at 2.83 and 3.0 A resolution, respectively. The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
crystal structure at 2.7 A resolution of the recombinant enzyme with active-site bound 5-formyl-tetrahydropteroylglutamate is obtained by soaking unliganded crystals of of the recombinant enzyme in 5-formyl-tetrahydropteroylglutamate, the conformation of the pteridine ring and its interactions with the enzyme differ slightly from those observed in complexes of the monoglutamate cofactor
-
hanging-drop vapour diffusion technique. Crystals of both mutants, E75L and E75Q are obtained by mixing 0.003v ml of an enzyme solution (34-44 mg/ml in 20 mM potassium phosphate, pH 7.3, with 1 mM dithiothreitol) with an equal volume of reservoir solution. The reservoir solution for E75L rcSHMT consists of 50 mM potassium phosphate, pH 6.6, 8.5-9.1% PEG 8000, and 100 mM KCl. For E75Q rcSHMT the reservoir solution consists of 15 mM potassium 2-(N-morpholino)ethanesulfonate, pH 6.4, 8.5-10% PEG 4000, and 30 mM KCl. Serine complexes are formed by adding 0.00025 ml of 250 mM L-serine directly to the drop
in complex with inhibitor, microbatch method, using 20-24% (w/v) PEG 4000, 0.06-0.12 M NaCl, 0.1 M Tris-HCl buffer, pH 8.5, and 10% (v/v) trifluoroethanol
purified enzyme in a binary complex with L-serine and in a ternary complex with D-serine and (6R)-5-formyltetrahydrofolate, microbatch method, mixing of 0.001 ml of 0.38 mM protein in 0.86 mM PLP, 62 mM 2-mercaptoethanol, 87 mM Gly, L-Ser, or D-Ser, and 43 mM tetrahydrofolate, with 0.001 ml of well solution containing 20-21% w/v PEG 4000, 70-90 mM NaCl, 100 mM Tris-HCl, pH 8.5, 15% v/v trifluoroethanol, 20°C, 1-4 days, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, molecular replacement
substrate binding structure analysis using crystal structure of the homodimeric PvSHMT in complex with D-serine and formyltetrahydrofolate, PDB ID 4OYT
-
purified recombinant enzyme in apoform, mixing of 200 nl of 10 mg/ml protein in 50 mM HEPES, pH 7.2, and 0.2 mM DTT with 200 nl of well solution containing 2M ammonium sulfate, 150 mM sodium chloride, and 100 mM sodium cacodylate, pH 6.5, 4°C, several days, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement and modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A244I
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
C83K
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
C83R
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
D304E
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
E160A/E193Q
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160C/E193Q
site-directed mutagenesis, the mutant shows 90% reduced activity compared to wild-type
E160D/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160E/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160F/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160G/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160H/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193A
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193C
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193D
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193F
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
E160I/E193G
site-directed mutagenesis, the mutant shows 10% increased activity compared to wild-type
E160I/E193H
site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type
E160I/E193I
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193K
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193L
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193M
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193N
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
E160I/E193P
site-directed mutagenesis, the mutant shows 70% decreased activity compared to wild-type
E160I/E193Q
site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type
E160I/E193R
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160I/E193S
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
E160I/E193T
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160I/E193V
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160I/E193W
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160I/E193Y
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
E160K
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
E160K/E193Q
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160L
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160L/E193Q
E160L/E193Q/E266M
site-directed mutagenesis, the mutant shows increased activity and thermostability compared to wild-type enzyme. The optimized strain BL21/pET28a-AdSHMTE160L/E193Q/E266M-5-UTR-REP3S16 s 106.06 g/l L-serine
E160M/E193Q
site-directed mutagenesis, the mutant shows activity similar to wild-type
E160N/E193Q
site-directed mutagenesis, the mutant shows highly increased activity compared to wild-type
E160P/E193Q
site-directed mutagenesis, the mutant shows 70% decreased activity compared to wild-type
E160Q
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
E160Q/E193Q
site-directed mutagenesis, the mutant shows highly increased activity compared to wild-type
E160R/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160S/E193Q
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
E160T/E193Q
site-directed mutagenesis, the mutant shows highly increased activity compared to wild-type
E160V/E193Q
site-directed mutagenesis, the mutant shows highly increased activity compared to wild-type
E160W/E193Q
site-directed mutagenesis, the mutant shows highly increased activity compared to wild-type
E160Y/E193Q
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type
E193K
site-directed mutagenesis, the mutant shows slightly increased thermal stability compared to wild-type
E193Q
site-directed mutagenesis, the mutant shows increased thermal stability and enzyme activity compared to wild-type
E266L
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
E266M
site-directed mutagenesis, rational design, the mutant shows highly increased thermal stability compared to wild-type
H341Y
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
N245E
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
S322K
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
S322T
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
T224I
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
T224M
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
T224V
site-directed mutagenesis, the mutant shows slightly increased thermal stability compared to wild-type
T380K
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
T380R
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
E266L
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
E266M
-
site-directed mutagenesis, rational design, the mutant shows highly increased thermal stability compared to wild-type
-
S322K
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
S322T
-
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
-
T224I
-
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
-
E266L
Alloalcanivorax dieselolei CGMCC 1.3690
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
E266M
Alloalcanivorax dieselolei CGMCC 1.3690
-
site-directed mutagenesis, rational design, the mutant shows highly increased thermal stability compared to wild-type
-
S322K
Alloalcanivorax dieselolei CGMCC 1.3690
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
S322T
Alloalcanivorax dieselolei CGMCC 1.3690
-
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
-
T224I
Alloalcanivorax dieselolei CGMCC 1.3690
-
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
-
E266L
Alloalcanivorax dieselolei DSM 16502
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
E266M
Alloalcanivorax dieselolei DSM 16502
-
site-directed mutagenesis, rational design, the mutant shows highly increased thermal stability compared to wild-type
-
S322K
Alloalcanivorax dieselolei DSM 16502
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
S322T
Alloalcanivorax dieselolei DSM 16502
-
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
-
T224I
Alloalcanivorax dieselolei DSM 16502
-
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
-
E266L
Alloalcanivorax dieselolei MCCC 1A00001
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
E266M
Alloalcanivorax dieselolei MCCC 1A00001
-
site-directed mutagenesis, rational design, the mutant shows highly increased thermal stability compared to wild-type
-
S322K
Alloalcanivorax dieselolei MCCC 1A00001
-
site-directed mutagenesis, the mutant shows thermal stability similar to wild-type
-
S322T
Alloalcanivorax dieselolei MCCC 1A00001
-
site-directed mutagenesis, the mutant shows increased thermal stability compared to wild-type
-
T224I
Alloalcanivorax dieselolei MCCC 1A00001
-
site-directed mutagenesis, the mutant shows decreased thermal stability compared to wild-type
-
L276A
L785A/L276A
the mutation has the effect of lowering the cooperativity of urea denaturation process
L85A
L85A/L276A
P214A
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.1fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 4°C higher than the wild-type value
P214G
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.3fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value
P216A
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.2fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5°C higher than the wild-type Tm-value, The Tm-value in presence of Ser is 0.5°C higher than the wild-type value
P216G
-
the turnover-number is 8.3fold lower than the wild-type value, the Km-value for Ser is 1.9fold higher than the wild-type value. The Km-value for tetrahydropteroylglutamate is 5.7fold higher than the wild-type value
P218A
-
the turnover-number is 1.1fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, double thermal transition that is considerably lower than wild-type enzyme, no increase in thermal stability upon binding serine
P218G
-
the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value
P258A
-
the turnover-number is below 0.5 per min, the KM-value for Ser is 26.7fold higher than the wild-type value
P264A
-
the turnover-number is 3fold lower than the wild-type value, the Km-value for Ser is 1.1fold higher than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value, Tm-value in absence of Ser is 9°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 11.5°C lower than the wild-type value
P264G
-
the turnover-number is 42.9fold lower than the wild-type value, the Km-value for Ser is 4.4fold higher than the wild-type value
E53Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
F351G
the mutation has no effect on tetrahydrofolate-independent and tetrahydrofolate-dependent activities
K226M
-
mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate per mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
K226Q
-
mutant enzymes is inactive, drastic rate of formation of the quinoid intermediate. It contains 1 mol of pyridoxal 5'-phosphate oer mol of subunit. pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K-226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
N341A
the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity
Y51F
-
the mutation results in a complete loss of tetrahydrofolate-dependent and tetrahydrofolate-independent activities
Y60A
the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity
Y61A
Y61F
-
site-directed mutagenesis, the bsSHMT mutant has lost aldolase activity to L-allo-threonine
I249L
the catalytic efficiency of the mutant is 2.78fold higher than that of the wild type enzyme
P285S
A206C
the mutation yields an enzyme that forms a 3-bromopyruvate-enzyme complex and is completely inactivated
H135N/R137A/E168N
tetrameric active mutant with a modified, less stable, tetrameric interface
L474F
-
shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
S394N
-
shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
Y105A
site-directed mutagenesis, the mutant enzyme is not inhibitable by the pyrrolo[3,2-d]pyrimidine inhibitors
Y105F
site-directed mutagenesis, increased enzyme inhibition potency by the pyrrolo[3,2-d]pyrimidine inhibitors with Phe105 SHMT2 is accompanied by increased growth inhibition of Phe105-expressing HCT116 cells compared to wild-type SHMT2. The mutant shows increased catalytic efficiency compared to wild-type
G132P
-
the mutant shows 301% activity compared to the wild type enzyme
H61G/G132P
-
the mutant shows 356% activity compared to the wild type enzyme
E75L
E75Q
L474F
shows normal values for kcat and Km for serine, shows lowered affinity (increased dissociation constant) for only the pentaglutamate form of the folate ligand, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
S394N
shows normal values for kcat and Km for serine, has increased dissociation constant values for both glycine and tetrahydrofolate and its pentaglutamate form compared to wild-type enzyme, shows decreased rates of pyridoxal phosphate addition to the mutant apo enzymes to form the active holo enzymes, thermal stability of SHMT or the rate at which it converts 5,10-methenyl tetrahydropteroyl pentaglutamate to 5-formyl tetrahydropteroyl pentaglutamate not affected
E74K
-
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild-type enzyme
E74Q
H147N
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
R262A
-
KM-value for L-Ser is 5.2fold higher than the wild-type value, the turnover-number is 5.25fold lower than the wild-type value, no transamination reaction with D-Ala, reaction with L-allo-Thr is 20fold decreased compared to wild-type value. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
S52A
-
KM-value for L-Ser is 1.3fold higher than the wild-type value, the turnover-number is 6fold lower than the wild-type value, transamination reaction with D-Ala is 20% of the wild-type activity, reaction with L-allo-Thr is 15% of the wild-type activity. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
S52C
-
KM-value for L-Ser is 11.2fold higher than the wild-type value, the turnover-number is 21fold lower than the wild-type value, no transamination reaction with D-Ala, no reaction with L-allo-Thr. L-Ser is unable to enhance the thermal stability as it does in wild-type enzyme
Y82F
-
95% loss of activity, kcat and Km decreased, a role in stabilizing the quinonoid intermediate
Y55T
K251Q
-
oligomeric structure not affected, but inactive in both the presence and absence of pyridoxal phosphate
K251R
-
oligomeric structure not affected, catalytic activity in the presence of pyridoxal phosphate also unaffected
additional information
E160L/E193Q
site-directed mutagenesis, the mutant shows 1.5fold higher activity compared to wild-type enzyme
E160L/E193Q
site-directed mutagenesis, the mutant shows 40% increased activity compared to wild-type
L276A
the mutation has the effect of lowering the cooperativity of urea denaturation process
L276A
the mutant is in the monomeric state and shows reduced activity
L276A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
L85A
the apo-L85A mutant enzyme is approximately 75% dimeric and shows reduced activity
L85A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
L85A/L276A
the mutant is in the monomeric state and shows reduced activity
L85A/L276A
-
site-directed mutagenesis, mutation in the third hydrophobic cluster. The decrease of hydrophobic contact area in the mutant causes a shift of the equilibrium between dimeric and monomeric forms in favor of the latter, pyridoxal 5'-phosphate binding stabilizes the dimeric form of the mutant
Y61A
-
the mutation results in a complete loss of tetrahydrofolate-dependent and tetrahydrofolate independent activities
Y61A
-
site-directed mutagenesis, the bsSHMT mutant has lost aldolase activity to L-allo-threonine
P285S
naturally occurring mutation of the conserved cis proline in isozyme SHMT8. Replacement of Pro285 by serine eliminates PLP-mediated catalytic activity of SHMT8, reduces folate binding, decreases enzyme stability, and affects the dimer-tetramer ratio of the enzyme in solution. The local reordering of the polypeptide chain extends an alpha-helix and shifts a turn region into the active site and causes dramatic structural perturbations
P285S
Glycine max F650
-
naturally occurring mutation of the conserved cis proline in isozyme SHMT8. Replacement of Pro285 by serine eliminates PLP-mediated catalytic activity of SHMT8, reduces folate binding, decreases enzyme stability, and affects the dimer-tetramer ratio of the enzyme in solution. The local reordering of the polypeptide chain extends an alpha-helix and shifts a turn region into the active site and causes dramatic structural perturbations
-
E75L
no activity with L-Ser and tetrahydrofolate. The mutant enzyme does not catalyze the formation of 5,10-methenyl-tetrahydropteroylglutamate or N5-hydroxymethylene-tetrahydropteroylglutamate
E75L
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
E75Q
500fold decrease in activity with L-Ser and tetrahydrofolate compared to wild-type enzyme, the KM-value for L-allothreonine is 10fold increased compared to wild-type value, the turnover-number for reaction with L-allothreonine is 4.3fold increased compared to wild-type enzyme
E75Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
E74Q
-
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild type enzyme
E74Q
-
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity
Y55T
the variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors
Y55T
-
the variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors
-
additional information
iterative saturating mutant library construction using coevolutionary analysis. Structural modeling and rational design screening of highly thermal stable AdSHMT mutants. Optimization and scale-up of L-serine conversion system
additional information
-
5-CHO-THF cycloligase mutant, doubled leaf 5-formyltetrahydrofolate level, little impact on SHMT activity, but glycine content of mutant leaves is 19fold higher than the wild-type, also a small accumulation of serine in the mutant relative to the wild-type
additional information
analysis of the phenotype and its rescue in shm1-2 T-DNA insertion mutant line, overview
additional information
-
analysis of the phenotype and its rescue in shm1-2 T-DNA insertion mutant line, overview
-
additional information
-
construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT frok Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding
additional information
-
generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview
additional information
-
SHMT activity controlled by Ptac, greatly reduced SHMT activity if no isopropyl-thio-beta-D-galactopyranoside is present, is explicitly prone to chromosomal mutations and rearrangements, thus making the strain unsuitable for large-scale fermentations
additional information
generation of a shmt mutant fly (shmtm3-5) using the CRISPR-Cas9 technique. Mutant shmtm3-5 has a 4 nucleotide deletion on exon 3 and is predicted to cause a frameshift from amino acid 120 that introduces a premature stop codon at amino acid 132, affecting all shmt isoforms. The mutation in shmtm3-5 is thus upstream of the enzyme conserved active site, which is predicted to start at amino acid 237. Mutant male animals do not survive to adulthood, males with the shmtm3-5 mutation (hemizygous animals) die in early pupal stages presenting a significant decrease of mRNA levels of shmt in shmtm3-5 compared with wild-type. Phenotype analysis, overview. Knockdown of shmt using RNA interference (RNAi) specifically in the neuroepithelia, with an embryonic neuroepithelia driver, R31H09-GAL4, the phenotype largely mimics the phenotype of shmtm3-5 mutant animals, causing disorganised optic lobes with almost no lamina or medulla neurons. Loss of shmt leads to smaller neuroepithelia, failure in lamina furrow formation and a reduced number of neuroblasts formed
additional information
-
mutant strain 1D19 from first round of DNA-shuffling, shows a 1.7fold increase in SHMT activity, mutant strain 2G31 from the second round of shuffling shows a 2.8fold increase in SHMT activity, mutant strain 3E7 from third round of shuffling, approximately 8fold increased enzyme activity and 41fold increased enzyme productivity as compared with its wild-type parent
additional information
-
immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution
additional information
-
mutant strain 1D19 from first round of DNA-shuffling, shows a 1.7fold increase in SHMT activity, mutant strain 2G31 from the second round of shuffling shows a 2.8fold increase in SHMT activity, mutant strain 3E7 from third round of shuffling, approximately 8fold increased enzyme activity and 41fold increased enzyme productivity as compared with its wild-type parent
-
additional information
-
immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution
-
additional information
-
construction of chimeric enzymes by swapping the structural domains between the bsSHMT from Bacillus subtilis and the bstSHMT from Bacillus stearothermophilus and generation of the two chimeric proteins bsbstc and bstbsc. The chimeras have secondary structure, tyrosine and pyridoxal 5'-phosphate microenvironment similar to that of the wild-type proteins. The chimeras show enzymatic activity slightly higher than that of the wild-type proteins.Unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding
additional information
-
generation of a chimera from Bacillus stearothermophilus and Bacillus subtilis SHMTs by domain swapping, quarternary structure analysis, overview
additional information
-
mutation of the consensus metal regulatory element sequence decreases the promoter activity of the -219 to -1 fragment by 60% in the absence of L-mimosine and attenuates L-mimosine inhibition by nearly 40%, mutation of the NF1 consensus sequence in the SHMT1 promoter -219 to -1 partially attenuates L-mimosine inhibition by ca. 20% without influencing SHMT1 promoter activity
additional information
SHMT2 knockdown in amplicon-positive RMS cells suppresses growth, transformation, and tumorigenesis, whereas overexpression in amplicon-negative RMS cells promotes these phenotypes. High SHMT2 expression reduces sensitivity of FP RMS cells to SHIN1, a direct SHMT2 inhibitor, but sensitizes cells to pemetrexed, an inhibitor of the folate cycle
additional information
SHMT2 knockdown leads to a loss of proliferation and viability across a panel of human DLBCL cell lines. Enzyme knockout via short hairpin against SHMT2 (shSHMT2_1 or shSHMT2_2)
additional information
generation of His-tagged truncated mutant SHMT2DELTAN30
additional information
enzyme knockout via short hairpin against SHMT2 (shSHMT2_1 or shSHMT2_2), phenotype, overview
additional information
-
the lcrp mutation is induced by treatment with N-methyl-N-nitrosourea (MNU), resulting in the reduction of prolamines and alpha-globulin levels in rice seeds. Mutant lcrp lines have a decreased level of CysR proteins, analysis of lcrp mutant lines EM49, EM811, EM1367, EM1593, and PM1031. Genotyping and DNA and amino acid sequence analysis of lcrp mutants, overview
additional information
generation of transgenic lines DUA1 (silicon-absorbing gene (Lsi1) is overexpressed in Dular rice) and Lsi1-OX, serine hydroxymethyltransferase is up-regulated in the transgenic rice, but down-regulated in the wild-type, and the expression of its corresponding miRNA changes in an opposite way, indicating that OsSHMT may be involved in regulating the chilling tolerance of Dular. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance, the transcription levels of histone H1 and nucleic acid binding protein are up-regulated in the Lsi1-OX rice. Lsi1-encoded protein OsNIP2;1 interacts with ATP synthase subunit beta, and the coordination of these proteins appears to function in reducing reactive oxygen species, as the H2O2 content of transgenic OsSHMT Arabidopsis thaliana is lower than that of the non-transgenic line under chilling treatment. ER-localised OsSHMT plays a role in scavenging H2O2 to enhance the chilling tolerance of Lsi1-OX rice, and ATP synthase subunit beta is an intermediate junction between OsNIP2;1 and OsSHMT. OsNIP2;1 is localised in the cytoplasm
additional information
sequencing of 12 Plasmodium vivax SHMT isolates reveals limited polymorphisms in 3 noncoding regions
additional information
-
sequencing of 12 Plasmodium vivax SHMT isolates reveals limited polymorphisms in 3 noncoding regions
additional information
in silico mutation of a conserved tyrosine residue that has role as FFO and PLG-binding and deletion of the unique fragment VSRQG of ITBSHMT_1 can change intramolecular interactions and/or cofactor binding affinity
additional information
-
in silico mutation of a conserved tyrosine residue that has role as FFO and PLG-binding and deletion of the unique fragment VSRQG of ITBSHMT_1 can change intramolecular interactions and/or cofactor binding affinity
-
additional information
the SaSHMT has the potential for industrial applications due to its tolerance of alkaline environment and a relatively high enzymatic conversion rate
additional information
-
the SaSHMT has the potential for industrial applications due to its tolerance of alkaline environment and a relatively high enzymatic conversion rate
additional information
the DELTAshmT knockout shows a decrease in intracellular bacterial cells as compared to the wild-type Staphylococcus aureus strain USA300, indicating that the shmT gene contributes to the survival of strain USA300 inside the host cells, and therefore, possibly plays an important role in the virulence and pathogenesis
additional information
-
the DELTAshmT knockout shows a decrease in intracellular bacterial cells as compared to the wild-type Staphylococcus aureus strain USA300, indicating that the shmT gene contributes to the survival of strain USA300 inside the host cells, and therefore, possibly plays an important role in the virulence and pathogenesis
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
-
the enzyme retains more than 50% of its activity after 30 min at pH 2.0-7.0
4 - 5
purified recombinant enzyme, loss of about 35% activity
5.5 - 8.5
the enzyme retains over 80% of the maximum activity over a pH range from 7.0 to 8.5 for 24 h at 4°C, and more than 70% of the maximal activity at pH 6.5. However, the enzyme exhibits a rapid decrease in activity at pH 5.5
5.5 - 9
purified recombinant SaSHMT shows significant stability under weakly acidic and alkaline environment at pH 6.5-9.0. Without any stabilizer at pH 6.5-9.0 for 96 h at 4°C over 80% of maximum activity is retained, at pH 5.5-6.0 less than 80% activity remains, the enzyme is unstable below pH 5.5
6 - 7
6 - 8
-
purified recombinant enzyme, over 60% maximal activity remains after 24 h at pH 6.0-7.5, 4°C, less than 20% of maximal activity at pH 8.0
7.2 - 8.3
-
stable, at pH 8.55: loss of activity, tetrameric holoenzyme dissociates into the dimeric form, at pH 9.3: complete dissociation
9.25
transition of SHM1 is between pH 8 and 11 and centered at about pH 9.25
additional information
6 - 7
purified recombinant enzyme, loss of about 20% activity
8
transition of SHM2 is between pH 6.5 and 11 and centered at about pH 8.0
additional information
-
recombinant wild-type bsSHMT and chimeric mutant enzyme are significantly higher susceptible to proteolysis into smaller protein fragments at pH 11 as compared to neutral pH
additional information
-
recombinant wild-type bstSHMT and chimeric mutant enzyme are only merginally susceptible to proteolysis into smaller protein fragments at pH 11 and at neutral pH
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
the enzyme retains more than 80% of its activity after 30 min at 20-40°C. After 30 min at 45-50°C, the enzyme shows about 30% residual activity. The enzyme shows about 30% activity after 30 min at pH 10-12
30 - 65
-
a broad sigmoidal transition between 30°C and 65°C having an apparent Tm of about 48°C is observed for the native dimeric SHMT molecule, SHMT is a noncooperative molecule which starts losing the structure from very low temperature (30°C) and loses most of ist secondary structure at relatively high temperature
35 - 55
after 1 h incubation under pH 7.5, the enzyme retains over 35% of its maximal activity from 35°C to 45°C, but less than 15% at 55°C
40
45 - 65
-
the wild type enzyme shows a rapid decrease (to less than 20%) in activity after 30 min at 55-65°C, and shows about 35% activity after 30 min at 45°C
50
55
60
65
70
additional information
40
Psychrobacter sp. ANT206
A0A7L7SZS9
purified recombinant enzyme, loss of 50% activity after 30 min
40
the enzyme retains over 45% of its maximal activity after incubation at 40°C for 3 h
50
Psychrobacter sp. ANT206
A0A7L7SZS9
purified recombinant enzyme, when the incubation temperature is higher than 50°C, the rPsSHMT activity decreases rapidly
55
-
Tm-value for wild-type enzyme and mutant enzymes R262A, S52C and S52A without ligands or with Gly as ligand. Tm-value for mutant enzymes mutant enzymes R262A, S52C and S52A with L-Ser as ligand
60
-
for 10 min, the native enzyme conserves about 40% of its activity, while the mutant 3E7 retains about 56% of its activity
60
Psychrobacter sp. ANT206
A0A7L7SZS9
purified recombinant enzyme, complete inactivation after 30 min
65
the melting temperature of the wild type enzyme is at 65°C
70
-
complete loss of activity after 6 min, enzyme-antibody complex: 30% loss of activity after 20 min
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
Tm values of enzyme and dimeric and tetrameric forms in the absence and presence of ligands
additional information
-
pyridoxal 5'-phosphate increases the thermal stability
additional information
-
L-serine increases the thermal stability
additional information
-
enzyme-antibody complex more stable to elevated temperatures than free enzyme, allosteric effectors fail to protect free enzyme
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
additional information
-
the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
Tm: 55°C, increased to 65°C in the presence of L-serine, Tm: 68°C mutant enzyme Y82F in the presence of serine
additional information
-
Tm of wild-type and mutant enzyme: 54°C, in the presence of serine Tm of wild-type enzyme: 63°C
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
additional information
-
glycerol, 30% v/v, enhances thermal stability
additional information
-
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
above 6 M urea the dichrpoic activity is reduced significantly with a transition midpoint at 2.56 M. This process is completely reversible
-
bsSHMT has six unconserved lysine residues in C-terminal domain which render it more resistant to alkaline denaturation. Chemical modification of lysine side chains results in stabilization of monomers
-
DTT stabilizes
EDTA stabilizes
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM1
guanidinium chloride-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations, SHM2
L-serine stabilizes
pyridoxal 5'-phosphate stabilizes
the kcat value of the enzyme in phosphate buffer is about 60% of that measured in HEPES buffer
-
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM1
urea-induced two-step unfolding of SHM1 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations. The enzyme-bound pyridoxal 5'-phosphate gets dissociated from the enzyme on treatment with about 1.25 M urea, SHM2
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway
-
unlike the wild-type enzyme bsSHMT, which undergoes dissociation of native dimer into monomers at low guanidinium chloride concentrations, resulting in a non-cooperative unfolding of the enzyme, its chimera bsbstc, having the C-terminal domain of bstSHMT is resistant to low guanidinium chloride concentration and shows a guanidinium-chloride-induced cooperative unfolding from native dimer to unfolded monomer. The wild-type dimeric bstSHMT is resistant to low guanidinium chloride concentrations and shows a guanidinium chloride-induced cooperative unfolding, whereas its chimera bstbsc, having the C-terminal domain of bsSHMT, shows dissociation of native dimer into monomer at low guanidinium chloride concentrations and a guanidinium-induced non-cooperative unfolding. The C-terminal domain of dimeric SHMT plays a vital role in stabilization of the oligomeric structure of the native enzyme hence modulating its unfolding pathway
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C (or -80°C), in the presence of 10% glycerol, for at least 6 months, no significant change in catalytic activity
-20°C, 6-8 months in the presence of pyridoxal 5'-phosphate, 2-mercaptoethanol, DTT and EDTA
-
0°C, at least 2 months in the presence of pyridoxal 5'-phosphate, 2-mercaptoethanol, DTT and EDTA
-
4°C, purified recombinant enzyme, 96 h, over 60% of maximal activity remains
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, gel filtration
by ammonium sulfate precipitation and gel filtration, more than 95% pure
chimeric enzymes
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephadex G-25 gel filtration
-
glutathione-Sepharose resin column chromatography and Superdex S200 gel filtration
-
HisTrap resin column chromatography and Superdex S200 gel filtration
Ni-Sepharose column chromatography, Sephadex G-25 gel filtration, and SP-Sepharose column chromatography
-
Ni2+-chelating column chromatography, SP Sepharose column chromatography and Superdex S200 gel filtration
partial by chloroplast preparation
polyethyleneimine precipitation, Q-Sepharose column chromatography and Sephacyl S-200 gel filtration
-
polyethyleneimine precipitation, SP-Sepharose column chromatography and DEAE-Sepharose column chromatography
-
recombinant C-terminally His-tagged enzyme from Escherichia coli by nickel affinity chroatography, dialysis, tag cleavage by PreScission protease, followed by anion exchange chromatography and gel filtration
recombinant enzyme
recombinant enzyme 11.2fold from Escherichia coli strain BL21(DE3) to homogeneity by polyethyleneimine precipitation, anion exchange chromatography, and gel filtration
recombinant enzyme from Escherichia coli strain BL21(DE3) by polyethyleneimine precipitation, anion and cation exchange chromatography
-
recombinant enzymes by tandem affinity purification, immunoprecipitation, heat treatment,
-
recombinant GST-tagged enzyme from Escherichia coli strain Bl21(DE3) by glutathione affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
Psychrobacter sp. ANT206
A0A7L7SZS9
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and dialysis
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography
recombinant His-tagged truncated mutant SHMT2DELTAN30 from Escherichia coli strain Rosetta (DE3)pLysS by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant N-terminally His-tagged enzyme from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant soluble His-tagged enzyme from Escherichia coli strain Rosetta 2(DE3) by nickel affinity chromatography
the His-tagged enzyme is purified by His GraviTrap column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
-
the pyridoxal-5'-phosphate-binding domain of SHMT is purified from inclusion bodies by rapid mixing followed by MonoQ column chromatography
-
using a 30 to 50% ammonium sulfate precipitation, gel filtration and chromatography on CM-Sephadex columns. From 2 liters of cells, approximately 43 mg of pure zmSHMT is obtained with an overall yield of 90%
by ammonium sulfate precipitation and gel filtration, more than 95% pure
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His6-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
both isoforms cloned in frame with EGFP at their C-terminus and transfected into Leishmania major
-
comparison
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli resulting in the increased accumulation of glycine and L-serine. Choline and glycine betaine levels are also significantly increased. Under high salinity, the growth rate of ApSHMT-expressing cells is faster compared to its respective control
efmSHMT, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli
enzyme expression in HCT-116 cells with inducible expression of wild-type and Y105F SHMT2, recombinant expression of His-tagged truncated mutant SHMT2DELTAN30 in Escherichia coli strain Rosetta (DE3)pLysS
Escherichia coli DH5alpha-PUC19 and Escherichia coli BL21 (DE3) used as host-vector system
-
expressed as fusion protein with an N-terminal Strep-tag in Escherichia coli strain BL21 Gold
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of a dominant negative, tetracycline-inducible SHMT1 protein, DN2-SHMT1, in HeLa and SH-SY5Y cells, expression of RFP-tagged SHMT2alpha and of YFP- or FLAG-tagged SHMT1
-
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3)
expression pattern of SHMT2 in 76 breast cancer patients after modified radical mastectomy, expression analysis
-
full-length cDNA clone SST18 encoding potato SHMT inserted in antisense orientation into the pBIN19 based vector L700 and introduced into the genome of Solanum tuberosum
-
gene glyA, cloning of ITBSHMT_1 (ITB serine hydroxylmethyltransferase clone number 1), phylogenetic analysis, recombinant expression of soluble His-tagged enzyme in Escherichia coli strain Rosetta 2(DE3)
gene glyA, codon optimization, recombinant expression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
-
gene glyA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, subcloning in Escherichia coli strain DH5alpha, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene glyA, DNA and amino acid sequence determination and analysis, phylogenetic tree, subcloning in Escherichia coli strain DH5alpha, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene glyA, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
Psychrobacter sp. ANT206
A0A7L7SZS9
gene glyA, DNa and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, sequence comparison, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
gene glyA, DNA and amino acid sequence determination and analysis, thermal asymmetric interlaced PCR, TAIL-PCR, sequence comparisons and phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene glyA, genome mining, codon optimization, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), AdSHMT expression optimization, method, overview
gene glyA, genomic cloning and recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3), subcloning in Escherichia coli strain DH5alpha, quantitative real-time PCR enzyme expression analysis
gene glyA, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain HMS174 (DE3)
gene glyA, recombinant expression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
gene LCRP, DNA and amino acid sequence determination and analysis, generation of a genetic linkage map of the LCRP gene
-
gene SHMT1, semiquantitative PCR and quantitative real-time PCR enzyme expression analysis
gene SHMT2, encoded in the 12q13-q14 chromosomal region, quantitative PCR enzyme expression analysis. Comparison of the expression of 12q13-q14 amplicons in fusion-positive (FP) rhabdomyosarcoma (RMS) with those of other cancer categories (glioblastoma multiforme, lung adenocarcinoma, and liposarcoma) in which 12q13-q14 amplification frequently occurs. Location of the 12q13-q14 amplicon across tumor types, overview
gene SHMT2, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) increasing the capability of Escherichia coli to grow in high salt conditions
gene SHMT2, SHMT2 localizes to the most frequent region of copy number gains at chromosome 12q14.1 in lymphoma
genes pfshmt and PF14_ 0534, encoding isozymes PfSHMTc and PfSHMTm, respectively, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged full-length isozymes
-
heterologously overproduced in Escherichia coli without a His6-tag
His6-tagged enzyme is expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
-
into pET43.1a vector and transformed into Escherichia coli HMS174(DE3) cells
Q2TL58
into pQE60 vector having C terminal His6-tag, expression in Escherichia coli M15 cells
mutations introduced into the cDNA for human cytosolic SHMT and expressed from an Escherichia coli expression system
-
mutations introduced into the cDNA for rabbit cytosolic SHMT and expressed from an Escherichia coli expression system
phylogenetic analysis, expression in Escherichia coli strain Rosetta, transient expression of EGFP-tagged full-length AtSHMT3 in Arabidopsis thaliana leaf protoplasts
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant soluble enzyme overexpression in Escherichia coli strain BL21(DE3)
using the AlkS/PalkB-expression system Escherichia colis serine hydroxymethyltransferase gene glyA is overexpressed in Escherichia coli. It is shown that the system is already fully turned on at inducer concentrations as low as 0.005% (v/v). The optimum induction procedure for production of serine hydroxymethyltransferase is elaborated. Volumetric and specific productivity are found to increase with specific growth rate in glucose-limited fed-batch cultures. Acetate excretion as a result of recombinant protein production can be avoided in an optimized fermentation protocol by switching earlier to a linear feed. A final cell dry weight (CDW) concentration of 52 g/l is reached producing recombinant GlyA with a maximum specific activity of 6.3 U/mg total protein
-
wild-type and mutant enzymes S52A, S52C and R262A are overexpressed in Escherichia coli
-
wild-type and mutants cloned into vector pET-29B and expressed in Escherichia coli BL21(DE3) cells, moreover expressed in Trichomonas vaginalis with a C-terminal HA tag
-
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3)
-
expression of wild-type and chimeric mutant in Escherichia coli strain BL21 (DE3)
-
gene glyA, recombinant expression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
gene glyA, recombinant expression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
gene glyA, recombinant expression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
gene SHMT2, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) increasing the capability of Escherichia coli to grow in high salt conditions
gene SHMT2, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) increasing the capability of Escherichia coli to grow in high salt conditions
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5-amino-4-imidazole carboxamide ribonucleotide 5'-phosphate stimulates the transcriptional expression of the enzyme
a non-lethal dose of UV-C radiation (10 mJ/cm2 UV (254 nm)) increases SHMT1 internal ribosome entry site activity and protein levels
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about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75%
endoplasmic reticulum stress-dependent regulation of the expression of serine hydroxymethyltransferase 2 in glioblastoma cells. Expression of the SHMT2 gene is not affected in U87MG cells after silencing of XBP1 and inhibition of ERN1 endoribonuclease alone
heterogeneous nuclear ribonucleoprotein H2 stimulates SHMT1 internal ribosome entry site activity by binding to the 5-untranslated region of the transcript and interacting with CUG-binding protein 1, CUG-binding protein 1 stimulates the internal ribosome entry site-mediated translation of SHMT1
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high salinity also strongly induces the transcript level of ApSHMT in Aphanothece halophytica
histone H1 and nucleic acid binding protein are found to bind to the promoter region of OsSHMT and regulate its expression
in mitochondria, ferredoxin-dependent glutamate synthase interacts physically with SHMT1, and this interaction is necessary for photorespiratory SHMT activity
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in NSCLC cells, long noncoding RNA (lncRNA) Gm15290 exerts a pro-oncogene effect by negatively regulating the expression of miR-615-5p and thus increasing the protein levels of miR-615-5p target genes, including SHMT2
inhibition of ERN1 endoribonuclease and protein kinase in glioblasxadtoma cells leads to a down-regulation of SHMT2 gene expression in U87MG cells
SHMT2 can be directly and negatively regulated by miR-370 in human articular chondrocytes and miR-615-5p in HCC cells
5-amino-4-imidazole carboxamide ribonucleotide 5'-phosphate stimulates the transcriptional expression of the enzyme
-
5-amino-4-imidazole carboxamide ribonucleotide 5'-phosphate stimulates the transcriptional expression of the enzyme
-
-
about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75%
-
about 3fold increase of SHMT activity during exponential growth with a further increase at the onset of the stationary phase, the essential SHMT has highest activity in the stationary phase and the regulator GlyR acts as an activator of transcription in this growth phase. Addition of glycine results in a slight but significant increase of SHMTactivity by 75%
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
5 ml of supernatant containing the solubilized domain is added drop by drop to 100 ml of stirring potassium phosphate buffer (50 mM, pH 7.4 containing 1 mM EDTA, 2 mM beta-mercaptoethanol, 0.1 mM pyridoxal 5'-phosphate, and 0.1 M NaCl)
-
denatured SHMT samples (0.023 mM in 8 M urea at 20°C) are able to recover after 4 h when kept with 8 M urea in 50 mM Na-HEPES, pH 7.2, containing 0.2 mM dithiothreitol and 0.1 mM EDTA for 15 h at 20°C
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
the AlkS/PalkB-expression system is shown as an efficient tool for the production of recombinant serine hydroxymethyltransferase in Escherichia coli fed-batch fermentations
drug development
medicine
pharmacology
-
L-serine is required for pharmaceutical purposes, availability of a sugar-based microbial process for its production is desirable, however, SHMT prevents overproduction of L-serine, control of the essential SHMT activity by a novel physiological approach
synthesis
additional information
analysis
-
SHMT1 is a zinc-inducible gene, provides first mechanism for the regulation of folate-mediated one-carbon metabolism by zinc
analysis
-
molecular dynamics simulations and interaction energy analysis for compounds designed as potential selective inhibitors of Plasmodium falciparum SHMT based on the conformational and dynamics differences observed between the residues Asp146 and Glu137 in the active sites of human SHMT and Plasmodium falciparum SHMT, respectively
analysis
molecular dynamics simulations and interaction energy analysis for compounds designed as potential selective inhibitors of Plasmodium falciparum SHMT based on the conformational and dynamics differences observed between the residues Asp146 and Glu137 in the active sites of human SHMT and Plasmodium falciparum SHMT, respectively
analysis
-
protein sequence of the two isoforms, the short form SHMT-S and the long form SHMT-L, show 59% identity
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the human enzyme is a potential target for cancer treatment
drug development
the enzyme might be a a key target for the development of chemotherapic agents
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
A0A069BAT4
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
the enzyme represents a potential target for chemotherapeutics
drug development
SHMT is considered a target for drugs through folate metabolism, especially for cancer and malaria
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
drug development
-
the enzyme represents a potential target for chemotherapeutics
-
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
enzyme is a potential target for cancer chemotherapy
medicine
-
enzyme is distinct from its prokaryotic and eukaryotic counterparts, thus is a potential drug target
medicine
ldSHMT is of medical importance as a drug target since ldSHMT is preferentially expressed in the amastigote stage of parasite which resides in human macrophages
medicine
-
ldSHMT is of medical importance as a drug target since ldSHMT is preferentially expressed in the amastigote stage of parasite which resides in human macrophages
-
synthesis
-
improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45°C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4%
synthesis
-
improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45°C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4%
-
additional information
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae
additional information
-
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae
additional information
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae
additional information
-
two conserved inserts of 3 and 31 amino acids, distinctive characteristics of the Chlamydiales order, ancient lateral gene transfers from actinobacteria to chlamydiae
EXTERNAL LINKS (specific for EC-Number 2.1.2.1)
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Release 2026.1 (March 2026)
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