EC number:1.14.99.52

Enzyme

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EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.99 Miscellaneous
ID:1.14.99.52
Description:L-cysteinyl-L-histidinylsulfoxide synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.99.52
BRENDA Enzyme Link: BRENDA 1.14.99.52
KEGG Enzyme Link: KEGG1.14.99.52
BioCyc Enzyme Link: BioCyc 1.14.99.52
ExPASy Enzyme Link: ExPASy1.14.99.52
EC2PDB Enzyme Link: EC2PDB 1.14.99.52
ExplorEnz Enzyme Link: ExplorEnz 1.14.99.52
PRIAM enzyme-specific profiles Link: PRIAM 1.14.99.52
IntEnz Enzyme Link: IntEnz 1.14.99.52
MEDLINE Enzyme Link: MEDLINE 1.14.99.52

EC number:1.14.99.52

MSA:

1.14.99.52;
Phylogenetic Tree:

1.14.99.52;
Uniprot:
M-CSA:
RHEA:42676 L-cysteine + L-histidine + O2 = H2O + L-alanin-3-yl L-histidin-5-yl sulfoxide
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]:[cH;+0:4]:[*:5].[O;H0;+0:6]=[O;H0;+0:7]>>[*:3]:[c;H0;+0:4](:[*:5])-[S;H0;+0:2](-[*:1])=[O;H0;+0:6].[OH2;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.Song H, Her AS, Raso F, Zhen Z, Huo Y, Liu P2014 Apr 1824684381
Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses.Song H, Leninger M, Lee N, Liu P2013 Sep 2024016264
Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis.Mashabela GT, Seebeck FP2013 Sep 1123877651
Identification and characterization of the first ovothiol biosynthetic enzyme.Braunshausen A, Seebeck FP2011 Feb 1621247153