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Information on EC 2.1.2.7 - D-alanine 2-hydroxymethyltransferase
for references in articles please use BRENDA:EC2.1.2.7
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.2 Hydroxymethyl-, formyl- and related transferases
2.1.2.7 D-alanine 2-hydroxymethyltransferase
IUBMB Comments
Also acts on 2-hydroxymethylserine.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
mshmt, alpha-methylserine hydroxymethyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methylserine hydroxymethyltransferase
-
-
-
-
alpha-methylserine hydroxymethyltransferase
hydroxymethyltransferase, 2-methylserine
-
-
-
-
MSHMT
alpha-methylserine hydroxymethyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase
Also acts on 2-hydroxymethylserine.
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CAS REGISTRY NUMBER
COMMENTARY
9075-76-7
-
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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
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
tetrahydrofolate + 2-ethyl-DL-serine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
Substrates: assay at pH 7.4, 30Ā°C
Products: -
Products: -
r
2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
Substrates: assay at pH 7.4, 30Ā°C
Products: -
Products: -
r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: stereospecific, dimedon cannot replace tetrahydrofolate
Products: -
Products: -
r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: stereospecific, dimedon cannot replace tetrahydrofolate
Products: 5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
Products: 5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: stereospecific, dimedon cannot replace tetrahydrofolate
Products: 5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
Products: 5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
-
Substrates: stereospecific
Products: -
Products: -
r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 2-ethyl-DL-serine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 2-ethyl-DL-serine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
-
Substrates: specific removal of one of the two hydroxyl groups
Products: -
Products: -
r
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
-
Substrates: -
Products: -
Products: -
?
tetrahydrofolate + 2-methyl-DL-serine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: -
Products: -
Products: -
r
tetrahydrofolate + 2-methyl-DL-serine
5,10-methylenetetrahydrofolate + D-alanine + H2O
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by Mg2+, Mn2+, Al3+, 2-mercaptoethanol
-
additional information
-
iodoacetate, GSH; no inhibition by Mg2+, Mn2+, Al3+, 2-mercaptoethanol
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Proteomic identification of mitochondrial targets of arginase in human breast cancer.
Neoplasms
Proteomic identification of mitochondrial targets of arginase in human breast cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
L-tetrahydrofolate
-
pH 7.5, calculated on the basis of one isomer
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
96% loss of activity after 10 min, hydroxymethylserine plus tetrahydrofolate and pyridoxal 5'-phosphate prevent
50
50
-
complete inactivation after 10 min, 55% loss of activity in the presence of tetrahydrofolate, pyridoxal 5'-phosphate plus hydroxymethylserine or D-serine
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tetrahydrofolate plus pyridoxal 5-phosphate plus hydroxymethylserine increase temperature-stability
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilson Miles, E.
alpha-Methylserine transhydroxymethylase (Pseudomonas)
Methods Enzymol.
17B
341-346
1971
Pseudomonas sp.
-
brenda
Wilson, E.M.; Snell, E.E.
Metabolism of alpha-methylserine. I. Alpha-methylserine hydroxymethyltransferase
J. Biol. Chem.
237
3171-3179
1962
Pseudomonas sp., Pseudomonas sp. MS
brenda
Wilson, E.M.; Snell, E.E.
Metabolism of alpha-methylserine. II. Stereospecificity of alpha-methylserine hydroxymethyltransferase
J. Biol. Chem.
237
3180-3184
1962
Pseudomonas sp.
brenda
Sperl, G.T.
Microbial metabolism of 2-methyl amino acids
Curr. Microbiol.
19
135-138
1989
Clostridium tetanomorphum, Escherichia coli
-
brenda
Nozaki, H.; Kuroda, S.; Watanabe, K.; Yokozeki, K.
Cloning of the gene encoding alpha-methylserine hydroxymethyltransferase from Aminobacter sp. AJ110403 and Ensifer sp. AJ110404 and characterization of the recombinant enzyme
Biosci. Biotechnol. Biochem.
72
3002-3005
2008
Aminobacter sp. AJ110403 (B2DEU8), Ensifer sp. AJ110404 (B2DEV1)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.2.7)
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Release 2023.1 (January 2023)
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