Functions of Genes and Enzymes Involved in Phenalinolactone Biosynthesis

Phenalinolactones are novel terpene glycoside antibiotics produced by Streptomyces sp. Tü6071. Inactivation of three oxygenase genes (plaO2, plaO3 and plaO5), two dehydrogenase genes (plaU, plaZ) and one putative acetyltransferase gene (plaV) led to the production of novel phenalinolactone derivativ...

Full description

Saved in:
Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2010-07, Vol.11 (10), p.1383-1391
Main Authors: Daum, Martina, Schnell, Hans-Jörg, Herrmann, Simone, Günther, Andreas, Murillo, Renato, Müller, Rolf, Bisel, Philippe, Müller, Michael, Bechthold, Andreas
Format: Article
Language:English
Subjects:
4-Butyrolactone - biosynthesis
Acetyltransferases - genetics
Acetyltransferases - metabolism
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biocatalysis
Cytochrome P-450 Enzyme System - metabolism
Dioxygenases - metabolism
Glycosides - biosynthesis
Glycosides - chemistry
Multigene Family
natural products
Oxidoreductases - genetics
Oxidoreductases - metabolism
oxygenases
Oxygenases - genetics
Oxygenases - metabolism
phenalinolacone
Streptomyces
Streptomyces - enzymology
Streptomyces - genetics
Terpenes - chemistry
Terpenes - metabolism
terpenoids
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Phenalinolactones are novel terpene glycoside antibiotics produced by Streptomyces sp. Tü6071. Inactivation of three oxygenase genes (plaO2, plaO3 and plaO5), two dehydrogenase genes (plaU, plaZ) and one putative acetyltransferase gene (plaV) led to the production of novel phenalinolactone derivatives (PL HS6, PL HS7, PL HS2 and PL X1). Furthermore, the exact biosynthetic functions of two enzymes were determined, and their in vitro activities were demonstrated. PlaO1, an FeII/α-ketoglutarate-dependent dioxygenase, is responsible for the key step in γ-butyrolactone formation, whereas PlaO5, a cytochrome P450-dependent monooxygenase, catalyses the 1-C-hydroxylation of phenalinolactone D. In addition, stable isotope feeding experiments with biosynthetic precursors shed light on the origin of the carbons in the γ-butyrolactone moiety.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201000117