|Gene:||glyA||Accession Number: G-3267 (MetaCyc)|
Species: Methylobacterium extorquens AM1
The serine hydroxymethyltransferase from M. extorquens has not been purified, and little is known about it. The gene glyA was cloned, and mutants which were disruppted in this gene were created. The mutants failed to grow on methanol, methylamine, ethanol, and ethylamine. Introduction of a plasmid with the cloned gene into the mutants restored wild type phenotype. The subunit structure of the enzyme or the size of its components were not studied.
Molecular Weight of Polypeptide: 46.3 kD (from nucleotide sequence)
pI: 6.0 [Chistoserdova94a]
Relationship Links: Entrez-Nucleotide:PART-OF:L33463
|Cellular Component:||GO:0005829 - cytosol|
|MultiFun Terms:||metabolism → carbon utilization → carbon compounds|
Enzymatic reaction of: serine hydroxymethyltransferase
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
This reaction is reversible.
Serine hydroxymethyltransferase catalyzes the reversible conversion of serine to glycine and tetrahydrofolate to 5,10-methylene tetrahydrofolate.
Chistoserdova94a: Chistoserdova LV, Lidstrom ME (1994). "Genetics of the serine cycle in Methylobacterium extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase." J Bacteriol 176(21);6759-62. PMID: 7961431
Trivedi02: Trivedi V, Gupta A, Jala VR, Saravanan P, Rao GS, Rao NA, Savithri HS, Subramanya HS (2002). "Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism." J Biol Chem 277(19);17161-9. PMID: 11877399
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