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Title 

Structural diversification of macrolactones by substrate-flexible cytochrome P450 monooxygenases

 

기질유연성을 갖는 사이토크롬 P450 모노옥시게나제에 의한 마크로락톤의 구조적 다양성

Authors 

S K LeeD B BasnetJ S J HongW S JungC Y ChoiH C LeeJ K SohngK G RyuD J KimJong Seog AhnB S KimH C OhD H ShermanY J Yoon

Publisher 

Wiley

Issue Date 

2005

Citation 

Advanced Synthesis & Catalysis, vol. 347, no. 10, pp. 1369-1378

Keywords 

cytochrome P450 monooxygenasehydroxylationmacrolidestreptomycessubstrate flexibility

Abstract 

The substrate flexibilities of several cytochrome P450 monooxygenases involved in macrolide biosynthesis were investigated to test their potential for the generation of novel macrolides. PikC hydroxylase in the pikromycin producer Streptomyces venezuelae accepted oleandomycin as an alternative substrate and introduced a hydroxy group at the C-4 position, which is different from the intrinsic C-12 hydroxylation position in the natural substrate. This is the first report of C-4 hydroxylation activity of cytochrome P450 monooxygenase involved in the biosynthesis of 14-membered macrolides. EryF hydroxylase from the erythromycin biosynthetic pathway of Saccharopolyspora erythraea and OleP oxidase from the oleandomycin biosynthetic pathway of Streptomyces antibioticus also showed a certain degree of plasticity towards alternative substrates. In particular, EryF and OleP were found to oxidize a 12-membered macrolactone as an alternative substrate. These results demonstrate the potential usefulness of these enzymes to diversify macrolactones by post-PKS oxidations.

ISSN 

1615-4150

Link 

http://dx.doi.org/10.1002/adsc.200404354

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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