| EC |
2.5.1.65 |
| Accepted name: |
O-phosphoserine sulfhydrylase |
| Reaction: |
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate |
| Other name(s): |
O-phosphoserine(thiol)-lyase |
| Systematic name: |
O-phospho-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase |
| Comments: |
A pyridoxal-phosphate protein. The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 1071505-11-7 |
| References: |
| 1. |
Mino, K. and Ishikawa, K. A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1. FEBS Lett. 551 (2003) 133–138. [DOI] [PMID: 12965218] |
| 2. |
Mino, K. and Ishikawa, K. Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J. Bacteriol. 185 (2003) 2277–2284. [DOI] [PMID: 12644499] |
| 3. |
Mino, K. and Ishikawa, K. Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 338–340. [PMID: 12554945] |
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| [EC 2.5.1.65 created 2004] |
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