Enzyme

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     2. Transferases
        2.5 Transferring alkyl or aryl groups, other than methyl groups
            2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
ID:2.5.1.65
Description:O-phosphoserine sulfhydrylase.
Alternative Name: O-phosphoserine(thiol)-lyase.
Cath: 3.90.1530.20; 3.40.50.1100;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.5.1.65
BRENDA Enzyme Link: BRENDA 2.5.1.65
KEGG Enzyme Link: KEGG2.5.1.65
BioCyc Enzyme Link: BioCyc 2.5.1.65
ExPASy Enzyme Link: ExPASy2.5.1.65
EC2PDB Enzyme Link: EC2PDB 2.5.1.65
ExplorEnz Enzyme Link: ExplorEnz 2.5.1.65
PRIAM enzyme-specific profiles Link: PRIAM 2.5.1.65
IntEnz Enzyme Link: IntEnz 2.5.1.65
MEDLINE Enzyme Link: MEDLINE 2.5.1.65
MSA:

2.5.1.65;

Phylogenetic Tree:

2.5.1.65;

Uniprot:
M-CSA:
RHEA:10252 H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + phosphate
RULE(radius=1) [*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[H+;H0:5].[SH2;+0:6]>>[*:1]-[CH2;+0:2]-[SH;+0:6].[*:4]-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
CysK2 from Mycobacterium tuberculosis is an O-phospho-L-serine-dependent S-sulfocysteine synthase.Steiner EM, Böth D, Lössl P, Vilaplana F, Schnell R, Schneider G2014 Oct25022854
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.Oda Y, Mino K, Ishikawa K, Ataka M2005 Aug 1216005886
A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1.Mino K, Ishikawa K2003 Sep 1112965218
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.Mino K, Ishikawa K2003 Apr12644499
Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1.Mino K, Oda Y, Ataka M, Ishikawa K2003 Feb12554945