Comparative functional characterization of a novel benzoate hydroxylase cytochrome P450 of Fusarium oxysporum

Title
Comparative functional characterization of a novel benzoate hydroxylase cytochrome P450 of Fusarium oxysporum
Author(s)
박현호프라딥라즈정은옥[정은옥]김병기[김병기]윤형돈[윤형돈]
Keywords
MOLECULAR CHARACTERIZATION; YEAST; REDUCTASE; EXPRESSION; GENES; OXYGENASES; BIOLOGY; SYSTEMS
Issue Date
201503
Publisher
ELSEVIER SCIENCE INC
Citation
ENZYME AND MICROBIAL TECHNOLOGY, v.70, pp.58 - 65
Abstract
FoCYP53A19, a novel cytochrome P450 capable of performing benzoate hydroxylation, was identified and characterized from the ascomycete Fusarium oxysporum f.sp. lycopersici. Comparative functional analysis of FoCYP53A19 with the heterologous and homologous cytochrome P450 reductases (CPR) such as Saccharomyces cerevisiae (ScCPR), Candida albicans (CaCPR) and F. oxysporum (FoCPR) revealed novel catalytic properties. The catalytic efficiency and substrate specificity of FoCYP53A19 were significantly influenced and altered by the source of the reductase employed. The yeast reconstitution system of FoCYP53A19 with ScCPR performed the hydroxylation of benzoic acid (BA) and demethylation of 3-methoxybenzoic acid (3-MBA); but when reconstituted with CaCPR, FoCYP53A19 performed only the essential hydroxylation of fungal benzoate catabolism. Remarkably, FoCYP53A19 with its homologous reductase FoCPR, not only demonstrated the improved conversion rates of BA and 3-MBA, but also exhibited activity toward the hydroxylation of 3-hydroxybenzoic acid. The electron transfer compatibility and the coupling efficiency between the homologous FoCYP-FoCPR system are significant and it favored enhanced monooxygenase activity with broader substrate specificity. (C) 2015 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/33249http://dx.doi.org/10.1016/j.enzmictec.2014.12.013
ISSN
0141-0229
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이과대학 > 화학생화학부 > Articles
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