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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
2-methylserine hydroxymethyltransferase, alpha-methylserine hydroxymethyltransferase, hydroxymethyltransferase, 2-methylserine, MSHMT,
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2-methylserine hydroxymethyltransferase
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alpha-methylserine hydroxymethyltransferase
hydroxymethyltransferase, 2-methylserine
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alpha-methylserine hydroxymethyltransferase
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alpha-methylserine hydroxymethyltransferase
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alpha-methylserine hydroxymethyltransferase
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MSHMT
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5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine
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hydroxymethyl group transfer
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5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase
Also acts on 2-hydroxymethylserine.
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2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
assay at pH 7.4, 30°C
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r
2-methyl-L-serine + tetrahydrofolate
D-alanine + 5,10-methylenetetrahydrofolate
assay at pH 7.4, 30°C
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r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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stereospecific, dimedon cannot replace tetrahydrofolate
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r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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stereospecific, dimedon cannot replace tetrahydrofolate
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r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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stereospecific, dimedon cannot replace tetrahydrofolate
5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
r
tetrahydrofolate + (+)-2-methylserine
5,10-methylenetetrahydrofolate + D-alanine + H2O
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stereospecific, dimedon cannot replace tetrahydrofolate
5,10-methylenetetrahydrofolate is non-enzymatically cleaved to tetrahydrofolate and formaldehyde
r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
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r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
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r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
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stereospecific
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r
tetrahydrofolate + (-)-ethylserine
5,10-methylenetetrahydrofolate + D-2-aminobutyrate + H2O
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r
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
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tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
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specific removal of one of the two hydroxyl groups
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r
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
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specific removal of one of the two hydroxyl groups
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r
tetrahydrofolate + 2-hydroxymethylserine
5,10-methylenetetrahydrofolate + D-serine + H2O
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pyridoxal 5'-phosphate
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Km: 0.01 mM at pH 7.5; requirement
pyridoxal 5'-phosphate
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requirement
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Cu2+
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at higher concentrations
DL-cycloserine
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strong, competitive
Fe2+
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at higher concentrations
Fe3+
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at higher concentrations
L-serine
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weak, competitive
p-chloromercuribenzoate
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Zn2+
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at higher concentrations
additional information
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no inhibition by Mg2+, Mn2+, Al3+, 2-mercaptoethanol
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additional information
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iodoacetate, GSH; no inhibition by Mg2+, Mn2+, Al3+, 2-mercaptoethanol
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6.2
2-ethyl-DL-serine
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pH 7.5
1.5
2-methyl-DL-serine
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pH 7.5
1.5 - 1.88
2-methyl-L-serine
0.8
hydroxymethylserine
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pH 7.5
0.25
L-tetrahydrofolate
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pH 7.5, calculated on the basis of one isomer
0.09 - 0.228
tetrahydrofolate
1.5
2-methyl-L-serine
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0.09
tetrahydrofolate
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0.002 - 0.0022
D-cycloserine
0.002
D-cycloserine
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additional information
4.75 U/mg, cell-free extract; 8.32 U/mg, after purification
additional information
1.25 U/mg, cell-free extract; 7.10 U/mg, after purification
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7.4
assay at
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6 - 10.5
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about half-maximal activity at pH 6.0 and 10.5
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assay at
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33 - 48
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about half-maximal activity at 33°C and 90% activity at 48°C
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UniProt
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UniProt
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inducible enzyme
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inducible enzyme
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B2DEU8_9RHIZ
425
0
45718
TrEMBL
B2DEV1_9RHIZ
425
0
45600
TrEMBL
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homodimer
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96% loss of activity after 10 min, hydroxymethylserine plus tetrahydrofolate and pyridoxal 5'-phosphate prevent
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value about
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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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prolonged dialysis inactivates
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pyridoxal 5-phosphate restores activity
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pyridoxal 5-phosphate stabilizes during purification
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tetrahydrofolate plus pyridoxal 5-phosphate plus hydroxymethylserine increase temperature-stability
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column chromatography, 16.4% yield
column chromatography, 72.8% yield
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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Wilson Miles, E.
alpha-Methylserine transhydroxymethylase (Pseudomonas)
Methods Enzymol.
17B
341-346
1971
Pseudomonas sp.
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Wilson, E.M.; Snell, E.E.
Metabolism of alpha-methylserine. I. Alpha-methylserine hydroxymethyltransferase
J. Biol. Chem.
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3171-3179
1962
Pseudomonas sp., Pseudomonas sp. MS
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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.
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Sperl, G.T.
Microbial metabolism of 2-methyl amino acids
Curr. Microbiol.
19
135-138
1989
Clostridium tetanomorphum, Escherichia coli
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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)
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2.1.2.7 D-alanine 2-hydroxymethyltransferase
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