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:1.14.99.50
Description:Gamma-glutamyl hercynylcysteine S-oxide synthase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.99.50
BRENDA Enzyme Link: BRENDA 1.14.99.50
KEGG Enzyme Link: KEGG1.14.99.50
BioCyc Enzyme Link: BioCyc 1.14.99.50
ExPASy Enzyme Link: ExPASy1.14.99.50
EC2PDB Enzyme Link: EC2PDB 1.14.99.50
ExplorEnz Enzyme Link: ExplorEnz 1.14.99.50
PRIAM enzyme-specific profiles Link: PRIAM 1.14.99.50
IntEnz Enzyme Link: IntEnz 1.14.99.50
MEDLINE Enzyme Link: MEDLINE 1.14.99.50
MSA:

1.14.99.50;

Phylogenetic Tree:

1.14.99.50;

Uniprot:
M-CSA:
RHEA:42672 hercynine + L-gamma-glutamyl-L-cysteine + O2 = H2O + L-gamma-glutamyl-hercynylcysteine S-oxide
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]:[cH;+0:4]:[*:5].[O;H0;+0:6]=[O;H0;+0:7]>>[*:1]-[S;H0;+0:2](=[O;H0;+0:6])-[c;H0;+0:4](:[*:3]):[*:5].[OH2;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.Seebeck FP2010 May 1920420449
Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway.Goncharenko KV, Vit A, Blankenfeldt W, Seebeck FP2015 Feb 2325597398
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system.Pluskal T, Ueno M, Yanagida M201424828577