We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00090Serine hydroxymethyltransferase pyridoxal-phosphate attachment site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00090
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
PROSITE method (with tools and information) covered by this documentation:
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 |
Copyright
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