| EC |
2.5.1.76 |
| Accepted name: |
cysteate synthase |
| Reaction: |
O-phospho-L-serine + sulfite = L-cysteate + phosphate |
| Other name(s): |
sulfite:O-phospho-L-serine sulfotransferase (phosphate-hydrolysing, L-cysteate-forming) |
| Systematic name: |
sulfite:O-phospho-L-serine sulfonotransferase (phosphate-hydrolysing, L-cysteate-forming) |
| Comments: |
A pyridoxal-phosphate protein. It is highly specific for O-phospho-L-serine and sulfite. The reaction proceeds through a dehydroalanine (2-aminoacrylic acid) intermediate. The enzyme from Methanosarcina acetivorans is evolutionarily related to threonine synthase (EC 4.2.3.1), but the reaction is more similar to that of O-phosphoserine sulfhydrylase (EC 2.5.1.65). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Graham, D.E., Taylor, S.M., Wolf, R.Z. and Namboori, S.C. Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase. Biochem. J. 424 (2009) 467–478. [DOI] [PMID: 19761441] |
|
| [EC 2.5.1.76 created 2009] |
| |
|
| |
|
Printable version