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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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.1.2.7
-
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RECOMMENDED NAME
GeneOntology No.
D-alanine 2-hydroxymethyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
One carbon pool by folate
-
-
Metabolic 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 hide
9075-76-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
B2DEU8
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
inducible enzyme
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
show the reaction diagram
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
show the reaction diagram
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
show the reaction diagram
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
at higher concentrations
DL-cycloserine
-
strong, competitive
Fe2+
-
at higher concentrations
Fe3+
-
at higher concentrations
L-Cycloserine
-
-
L-serine
-
weak, competitive
p-chloromercuribenzoate
-
-
Zn2+
-
at higher concentrations
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.2
2-ethyl-DL-serine
-
pH 7.5
1.5
2-methyl-DL-serine
-
pH 7.5
1.5 - 1.88
2-methyl-L-serine
0.8
hydroxymethylserine
-
pH 7.5
0.25
L-tetrahydrofolate
-
pH 7.5, calculated on the basis of one isomer
0.09 - 0.228
tetrahydrofolate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.0022
D-cycloserine
0.005
L-Cycloserine
-
-
5.6
L-serine
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
-
about half-maximal activity at pH 6.0 and 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33 - 48
-
about half-maximal activity at 33°C and 90% activity at 48°C
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
B2DEU8;
gel filtration
80000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
B2DEU8;
-
702735
6 - 7.5
-
702735
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
96% loss of activity after 10 min, hydroxymethylserine plus tetrahydrofolate and pyridoxal 5'-phosphate prevent
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged dialysis inactivates
-
pyridoxal 5-phosphate restores activity
-
pyridoxal 5-phosphate stabilizes during purification
-
tetrahydrofolate plus pyridoxal 5-phosphate plus hydroxymethylserine increase temperature-stability
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
column chromatography, 16.4% yield
column chromatography, 72.8% yield
B2DEU8;
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.2.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)