Glycine hydroxymethyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a glycine hydroxymethyltransferase (EC 2.1.2.1) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate + glycine + H₂O $\rightleftharpoons$ tetrahydrofolate + L-serine

The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, glycine, and H₂O, whereas its two products are tetrahydrofolate and L-serine.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase. Other names in common use include serine aldolase, threonine aldolase, serine hydroxymethylase, serine hydroxymethyltransferase, allothreonine aldolase, L-serine hydroxymethyltransferase, L-threonine aldolase, serine hydroxymethyltransferase, and serine transhydroxymethylase. This enzyme participates in 5 metabolic pathways: glycine, serine and threonine metabolism, lysine degradation, cyanoamino acid metabolism, one carbon pool by folate, and methane metabolism. It employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes 1BJ4, 1DFO, 1EJI, 1EQB, 1KKJ, 1KKP, 1KL1, 1KL2, 1LS3, 1RV3, 1RV4, 1RVU, 1RVY, 1YJS, 1YJY, 1YJZ, 2A7V, and 2DKJ.

[edit] References

IUBMB entry for 2.1.2.1
BRENDA references for 2.1.2.1 (Recommended.)
PubMed references for 2.1.2.1
PubMed Central references for 2.1.2.1
Google Scholar references for 2.1.2.1
Akhtar M, el-Obeid HA (1972). "Inactivation of serine transhydroxymethylase and threonine aldolase activities". Biochim. Biophys. Acta. 258: 791–9. PMID 5017703.
Blakley RL (1960). "A spectrophotometric study of the reaction catalysed by serine transhydroxymethylase". Biochem. J. 77: 459–65. PMID 16748851.
Fujioka M (1969). "Purification and properties of serine hydroxymethylase from soluble and mitochondrial fractions of rabbit liver". Biochim. Biophys. Acta. 185: 338–49. PMID 5808700.
Kumagai H, Nagate T, Yoshida H, Yamada H (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochim. Biophys. Acta. 258: 779–90. PMID 5017702.
Schirch L, Gross T (1968). "Serine transhydroxymethylase. Identification as the threonine and allothreonine aldolases". J. Biol. Chem. 243: 5651–5. PMID 5699057.