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2.5.1.65 |
Description |
O-phosphoserine sulfhydrylase |
Alternative names |
O-phosphoserine(thiol)-lyase;
Cysteine synthase (archaeal type) |
Catalyzed reaction |
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate |
Cofactor |
Pyridoxal phosphate. |
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. |
PDB |
1WKV; |
Organisms |
-Archea |
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Family |
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Links |
Enzyme (activities) 2.5.1.65
BRENDA (activities) 2.5.1.65
KEGG (pathways) 2.5.1.65
PLPMDB (PLP mutants) 2.5.1.65
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References |
Oda, Y.; Mino, K.; Ishikawa, K.; Ataka, M.
(2005) Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution J Mol Biol 351 334-44. Mino, K.; Ishikawa, K. (2003) A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1 FEBS Lett 551 133-8. Mino, K.; Ishikawa, K. (2003) Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1 J Bacteriol 185 2277-84. Articles on 2.5.1.65 |
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last changed |
2009/07/07 12:02 |
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