Journal Article

PUBDB-2015-06311

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis

Luhavaya, H. ; Dias, M. V. B. ; Williams, S. R. ; Hong, H. ; deOliveira, L. G. ; Leadlay, P. F. (Corresponding author)

2015
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/anie.201507090  doi:10.3204/PUBDB-2015-06311

Abstract: Tetrahydropyran rings are a common feature of complex polyketide natural products, but much remains to be learned about the enzymology of their formation. The enzyme SalBIII from the salinomycin biosynthetic pathway resembles other polyether epoxide hydrolases/cyclases of the MonB family, but SalBIII plays no role in the conventional cascade of ring opening/closing. Mutation in the salBIII gene gave a metabolite in which ring A is not formed. Using this metabolite in vitro as a substrate analogue, SalBIII has been shown to form pyran ring A. We have determined the X-ray crystal structure of SalBIII, and structure-guided mutagenesis of putative active-site residues has identified Asp38 and Asp104 as an essential catalytic dyad. The demonstrated pyran synthase activity of SalBIII further extends the impressive catalytic versatility of α+β barrel fold proteins.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)
2. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2015

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Database coverage:
; ; ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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