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New Reactions and Products Resulting from Alternative Interactions between the P450 Enzyme and Redox Partners
Zhang, Wei1,2; Liu, Yi1,2,3; Yan, Jinyong1,2; Cao, Shaona1,2; Bai, Fali1,2; Yang, Ying1,2; Huang, Shaohua1,2; Yao, Lishan1,2; Anzai, Yojiro4; Kato, Fumio4; Podust, Larissa M.5,6; Sherman, David H.7,8,9; Li, Shengying1,2
2014-03-05
Source PublicationJOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume136Issue:9Pages:3640-3646
Abstract

Cytochrome P450 enzymes are capable of catalyzing a great variety of synthetically useful reactions such as selective C-H functionalization. Surrogate redox partners are widely used for reconstitution of P450 activity based on the assumption that the choice of these auxiliary proteins or their mode of action does not affect the type and selectivity of reactions catalyzed by P450s. Herein, we present an exceptional example to challenge this postulate. MycG, a multifunctional biosynthetic P450 monooxygenase responsible for hydroxylation and epoxidation of 16-membered ring macrolide mycinamicins, is shown to catalyze the unnatural N-demethylation(s) of a range of mycinamicin substrates when partnered with the free Rhodococcus reductase domain RhFRED or the engineered Rhodococcus-spinach hybrid reductase RhFRED-Fdx. By contrast, MycG fused with the RhFRED or RhFRED-Fdx reductase domain mediates only physiological oxidations. This finding highlights the larger potential role of variant redox partner protein-protein interactions in modulating the catalytic activity of P450 enzymes.

SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
DOI10.1021/ja4130302
WOS KeywordSTREPTOMYCES-COELICOLOR A3(2) ; CYTOCHROME-P450 ENZYMES ; MACROLIDE ANTIBIOTICS ; MICROMONOSPORA-GRISEORUBIDA ; ACTIVE-SITE ; BIOSYNTHESIS ; MYCINAMICIN ; DOMAIN ; B(5) ; GENE
Indexed BySCI
Language英语
WOS Research AreaChemistry
WOS SubjectChemistry, Multidisciplinary
WOS IDWOS:000332684700045
Citation statistics
Cited Times:34[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qibebt.ac.cn/handle/337004/6243
Collection酶工程研究组
Affiliation1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, CAS Key Lab Biofuels, Qingdao 266101, Shandong, Peoples R China
2.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Qingdao 266101, Shandong, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Toho Univ, Fac Pharmaceut Sci, Chiba 2748510, Japan
5.Univ Calif San Francisco, Ctr Discovery & Innovat Parasit Dis, San Francisco, CA 94158 USA
6.Univ Calif San Francisco, Dept Pathol, San Francisco, CA 94158 USA
7.Univ Michigan, Dept Med Chem, Inst Life Sci, Ann Arbor, MI 48109 USA
8.Univ Michigan, Dept Chem, Inst Life Sci, Ann Arbor, MI 48109 USA
9.Univ Michigan, Dept Microbiol & Immunol, Inst Life Sci, Ann Arbor, MI 48109 USA
Recommended Citation
GB/T 7714
Zhang, Wei,Liu, Yi,Yan, Jinyong,et al. New Reactions and Products Resulting from Alternative Interactions between the P450 Enzyme and Redox Partners[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2014,136(9):3640-3646.
APA Zhang, Wei.,Liu, Yi.,Yan, Jinyong.,Cao, Shaona.,Bai, Fali.,...&Li, Shengying.(2014).New Reactions and Products Resulting from Alternative Interactions between the P450 Enzyme and Redox Partners.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,136(9),3640-3646.
MLA Zhang, Wei,et al."New Reactions and Products Resulting from Alternative Interactions between the P450 Enzyme and Redox Partners".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 136.9(2014):3640-3646.
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