| Serine hydroxymethyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Serine hydroxymethyltransferase 1 (cytosolic), homotetramer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.2.1 | ||||||||
| CAS no. | 9029-83-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-methylenetetrahydrofolate (5,10-CH2-THF).[1] This reaction provides the largest part of the one-carbon units available to the cell.[2]
- ^ Appaji Rao N, Ambili M, Jala VR, Subramanya HS, Savithri HS (April 2003). "Structure-function relationship in serine hydroxymethyltransferase". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 24–29. doi:10.1016/s1570-9639(03)00043-8. PMID 12686103.
- ^ Stover P, Schirch V (August 1990). "Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate". The Journal of Biological Chemistry. 265 (24): 14227–14233. doi:10.1016/S0021-9258(18)77290-6. PMID 2201683.