The role of erythromycin C-12 hydroxylase, EryK, as a substitute for PikC hydroxylase in pikromycin biosynthesis

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Title
The role of erythromycin C-12 hydroxylase, EryK, as a substitute for PikC hydroxylase in pikromycin biosynthesis
Author(s)
S K Lee; D B Basnet; C Y Choi; J K Sohng; Jong Seog Ahn; Y J Yoon
Bibliographic Citation
Bioorganic Chemistry, vol. 32, no. 6, pp. 549-559
Publication Year
2004
Abstract
The substrate flexibility of the erythromycin C-12 hydroxylase from Saccharopolyspora erythraea, EryK, was investigated to test its potential for the generation of novel polyketide structures. We have shown that EryK can accept the substrates of PikC from Streptomyces venezuelae which is responsible for the hydroxylation of YC-17 and narbomycin. In a S. venezuelae pikC deletion mutant, EryK could catalyze the hydroxylation of YC-17 and narbomycin to generate methymycin/neomethymycin and pikromycin, respectively. Molecular modeling of the enzyme-substrate complex suggested the possible interaction of EryK with alternative substrates. The results indicate that EryK is flexible toward some alternative polyketides and can be useful for structural diversification of macrolides by post-polyketide synthase hydroxylation.
Keyword
cytochrome P450 monooxygenasesEryKPikCpolyketide
ISSN
0045-2068
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bioorg.2004.06.002
Type
Article
Appears in Collections:
Ochang Branch Institute > Anticancer Agent Research Center > 1. Journal Articles
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