Entry
Name
L-cysteinyl-L-histidinylsulfoxide synthase;
OvoA
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
BRITE hierarchy
Sysname
L-histidine,L-cysteine:oxygen [S-(L-histidin-5-yl)-L-cysteine S-oxide-forming]
Reaction(IUBMB)
L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O [RN:
R11015 ]
Reaction(KEGG)
Substrate
Product
S-(L-histidin-5-yl)-L-cysteine S-oxide [CPD:
C20993 ];
H2O [CPD:
C00001 ]
Comment
Requires Fe2+ for activity. The enzyme participates in ovothiol biosynthesis. It also has some activity as EC
1.13.11.20 , cysteine dioxygenase, and can perform the reaction of EC
1.14.99.50 , gamma-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4].
History
EC 1.14.99.52 created 2015
Reference
Authors
Braunshausen A, Seebeck FP
Title
Identification and characterization of the first ovothiol biosynthetic enzyme.
Journal
Reference
Authors
Song H, Leninger M, Lee N, Liu P
Title
Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses.
Journal
Reference
Authors
Mashabela GT, Seebeck FP
Title
Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis.
Journal
Reference
Authors
Song H, Her AS, Raso F, Zhen Z, Huo Y, Liu P
Title
Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.
Journal
Other DBs