The Enzyme Database

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EC 1.16.3.3     
Accepted name: manganese oxidase
Reaction: 4 Mn2+ + 2 O2 + 4 H2O = 4 MnIVO2 + 8 H+ (overall reaction)
(1a) 4 Mn2+ + O2 + 4 H+ = 4 Mn3+ + 2 H2O
(1b) 4 Mn3+ + O2 + 6 H2O = 4 MnIVO2 + 12 H+
Other name(s): mnxG (gene name); mofA (gene name); moxA (gene name); cotA (gene name)
Systematic name: manganese(II):oxygen oxidoreductase
Comments: The enzyme, which belongs to the multicopper oxidase family, is found in many bacterial strains. It oxidizes soluble manganese(II) to insoluble manganese(IV) oxides. Since the enzyme is localized to the outer surface of the cell, its activity usually results in encrustation of the cells by the oxides. The physiological function of bacterial manganese(II) oxidation remains unclear.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Corstjens, P.L.A.M., de Vrind, J.P.M., Goosen, T. and de Vrind-de Jong, E.W. Identification and molecular analysis of the Leptothrix discophora SS-1 mofA gene, a gene putatively encoding a manganese-oxidizing protein with copper domains. Geomicrobiol. J. 14 (1997) 91–108.
2.  Francis, C.A., Casciotti, K.L. and Tebo, B.M. Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp. strain SG-1. Arch. Microbiol. 178 (2002) 450–456. [PMID: 12420165]
3.  Ridge, J.P., Lin, M., Larsen, E.I., Fegan, M., McEwan, A.G. and Sly, L.I. A multicopper oxidase is essential for manganese oxidation and laccase-like activity in Pedomicrobium sp. ACM 3067. Environ Microbiol 9 (2007) 944–953. [PMID: 17359266]
4.  Geszvain, K., McCarthy, J.K. and Tebo, B.M. Elimination of manganese(II,III) oxidation in Pseudomonas putida GB-1 by a double knockout of two putative multicopper oxidase genes. Appl. Environ. Microbiol. 79 (2013) 357–366. [PMID: 23124227]
5.  Su, J., Bao, P., Bai, T., Deng, L., Wu, H., Liu, F. and He, J. CotA, a multicopper oxidase from Bacillus pumilus WH4, exhibits manganese-oxidase activity. PLoS One 8:e60573 (2013). [PMID: 23577125]
[EC 1.16.3.3 created 2017]
 
 


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