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 |
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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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 24684381] |
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[EC 1.14.99.52 created 2015] |
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