The animal fatty acid synthase: one gene, one polypeptide, seven enzymes

S Smith - The FASEB journal, 1994 - Wiley Online Library
The animal fatty acid synthase comprises two multifunctional polypeptide chains, each
containing seven discrete functional domains, juxtaposed head‐to‐tail such that two …

PKS and NRPS release mechanisms

L Du, L Lou - Natural product reports, 2010 - pubs.rsc.org
Covering: up to September 2009 This review covers the recent literature on the release
mechanisms for polyketides and nonribosomal peptides produced by microorganisms. The …

New PCR primers for the screening of NRPS and PKS-I systems in actinomycetes: detection and distribution of these biosynthetic gene sequences in major taxonomic …

A Ayuso-Sacido, O Genilloud - Microbial ecology, 2005 - Springer
Nonribosomal peptide synthetases (NRPS) and type I polyketide synthases (PKS-I) are
biosynthetic systems involved in the synthesis of a large number of important biologically …

Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel “unnatural” natural products

R McDaniel, A Thamchaipenet… - Proceedings of the …, 1999 - National Acad Sciences
The structures of complex polyketide natural products, such as erythromycin, are
programmed by multifunctional polyketide synthases (PKSs) that contain modular …

The type I fatty acid and polyketide synthases: a tale of two megasynthases

S Smith, SC Tsai - Natural product reports, 2007 - pubs.rsc.org
Covering: up to the end of 2006 This review chronicles the synergistic growth of the fields of
fatty acid and polyketide synthesis over the last century. In both animal fatty acid synthases …

Methods for in silico prediction of microbial polyketide and nonribosomal peptide biosynthetic pathways from DNA sequence data

BO Bachmann, J Ravel - Methods in enzymology, 2009 - Elsevier
Foreknowledge of the secondary metabolic potential of cultivated and previously
uncultivated microorganisms can potentially facilitate the process of natural product …

Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine

A Witkowski, AK Joshi, Y Lindqvist, S Smith - Biochemistry, 1999 - ACS Publications
β-Ketoacyl synthases involved in the biosynthesis of fatty acids and polyketides exhibit
extensive sequence similarity and share a common reaction mechanism, in which the …

A tylosin ketoreductase reveals how chirality is determined in polyketides

AT Keatinge-Clay - Chemistry & biology, 2007 - cell.com
Because it controls the majority of polyketide stereocenters, the ketoreductase (KR) is a
central target in engineering polyketide synthases (PKSs). To elucidate the mechanisms of …

Conserved amino acid residues correlating with ketoreductase stereospecificity in modular polyketide synthases

P Caffrey - ChemBioChem, 2003 - Wiley Online Library
[8] TW Wiegand, RC Janssen, BE Eaton, Chem. Biol. 1997, 4, 675±683.[9] B. Zhang, TR
Cech, Chem. Biol. 1998, 5, 539±553.[10] GP Anderson, K. Shinagawa, Curr. Opin. Anti …

The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal …

L Du, C Sánchez, M Chen, DJ Edwards, B Shen - Chemistry & biology, 2000 - cell.com
Background: The structural and catalytic similarities between modular nonribosomal peptide
synthetases (NRPSs) and polyketide synthases (PKSs) inspired us to search for a hybrid …