IntEnz

EC 2.5.1.65 - O-phosphoserine sulfhydrylase

IntEnz Enzyme Nomenclature
EC 2.5.1.65

Names

Reaction

• 10252 [IUBMB]
  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  hydrogen sulfide

  hydrogen sulfide

  Name origin: UniProt - CHECKED (C)

  CHEBI:29919

  Formula: HS
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  O-phospho-L-serine

  O-phospho-L-serine

  Name origin: UniProt - CHECKED (C)

  CHEBI:57524

  Formula: C3H6NO6P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  =

  L-cysteine

  L-cysteine

  Name origin: UniProt - CHECKED (C)

  CHEBI:35235

  Formula: C3H7NO2S
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  phosphate

  phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:43474

  Formula: HO4P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Cofactor

• pyridoxal 5'-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.

Links to other databases

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: 133-138 (2003). [PMID: 12965218]
2. Mino, K. and Ishikawa, K.
   Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
   J. Bacteriol. 185: 2277-2284 (2003). [PMID: 12644499]
3. Mino, K., Oda, Y., Ataka, M. and Ishikawa, K.
   Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
   Acta Crystallogr. D Biol. Crystallogr. 59: 338-340 (2003). [PMID: 12554945]

[EC 2.5.1.65 created 2004]