PROSITE documentation PDOC00090Serine hydroxymethyltransferase pyridoxal-phosphate attachment site
Description
Serine hydroxymethyltransferase (EC 2.1.2.1) (SHMT) [1] catalyzes the transfer of the hydroxymethyl group of serine to tetrahydrofolate to form 5,10-methylenetetrahydrofolate and glycine. In vertebrates, it exists in a cytoplasmic and a mitochondrial form whereas only one form is found in prokaryotes. Serine hydroxymethyltransferase is a pyridoxal-phosphate containing enzyme. The pyridoxal-P group is attached to a lysine residue around which the sequence is highly conserved in all forms of the enzyme.
Last update:April 2006 / Pattern revised.
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Technical section
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Reference
| 1 | Authors | Usha R. Savithri H.S. Rao N.A. |
| Title | The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases. | |
| Source | Biochim. Biophys. Acta 1204:75-83(1994). | |
| PubMed ID | 8305478 |
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