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Title 

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

Authors 

S K LeeD B BasnetC Y ChoiJ K SohngJong Seog AhnY J Yoon

Publisher 

Elsevier

Issue Date 

2004

Citation 

Bioorganic Chemistry, vol. 32, no. 6, pp. 549-559

Keywords 

cytochrome P450 monooxygenasesEryKPikCpolyketideerythromycin Cmacrolidemethymycinnarbomycinneomethymycinoxygenase

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.

ISSN 

0045-2068

Link 

http://dx.doi.org/10.1016/j.bioorg.2004.06.002

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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