The Enzyme Database

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EC 1.14.99.52     
Accepted name: L-cysteinyl-L-histidinylsulfoxide synthase
Reaction: L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
For diagram of ergothioneine and ovothiol biosynthesis, click here
Glossary: S-(L-histidin-5-yl)-L-cysteine S-oxide = 5-{[(2R)-2-amino-2-carboxyethyl]sulfinyl}-L-histidine
Other name(s): OvoA
Systematic name: L-histidine,L-cysteine:oxygen [S-(L-histidin-5-yl)-L-cysteine S-oxide-forming]
Comments: 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, γ-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Braunshausen, A. and Seebeck, F.P. Identification and characterization of the first ovothiol biosynthetic enzyme. J. Am. Chem. Soc. 133 (2011) 1757–1759. [PMID: 21247153]
2.  Song, H., Leninger, M., Lee, N. and Liu, P. Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses. Org. Lett. 15 (2013) 4854–4857. [PMID: 24016264]
3.  Mashabela, G.T. and Seebeck, F.P. Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis. Chem. Commun. (Camb.) 49 (2013) 7714–7716. [PMID: 23877651]
4.  Song, H., Her, A.S., Raso, F., Zhen, Z., Huo, Y. and Liu, P. Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis. Org. Lett. 16 (2014) 2122–2125. [PMID: 24684381]
[EC 1.14.99.52 created 2015]
 
 


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