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A multifunctional polyketide-peptide synthetase essential for albicidin biosynthesis in Xanthomonas albilineans

Article Abstract:

Research reveals that albicidin biosynthesis is mediated by the polyketide synthase that is linked to a non-ribosomal peptide synthetase encoded by the xabB gene in Xanthomonas albilineans. Data show that the multifunctional enzyme is the largest reported polyketide- peptide synthetase and contains twelve catalytic domains.

Author: Huang, Guozhong, Zhang, Lianhui, Birch, Robert G.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
Australia, Singapore, Statistical Data Included, Physiological aspects, Enzymes, Enzyme synthesis, Polyketides, Plant toxins

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A gene from Alcaligenes denitrificans that confers albicidin resistance by reversible antibiotic binding

Article Abstract:

Soil isolates of Alcaligenes denitrificans express the albicidin resistance gene albB that codes for a 23 kDa protein that detoxifies albicidin through reversible binding. Partial DNA sequence homology is present between regions of the 621 bp coding domain and the albicidin resistance gene albA of Kelbsiella oxytoca. The albicidin resistance AlbR proteins from the two bacteria exhibit N-terminal homology but utilize varying codons for shared amino acids. Detection analysis, albicidin binding by a synthetic oligopeptide and translational fusions indicate the N-terminal region as a functional domain.

Author: Birch, Robert G., Basnayake, W.V. Shiromi
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Research, Analysis, Drug resistance in microorganisms, Microbial drug resistance, Nucleotide sequence, Base sequence, Bacteria

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High affinity binding of albicidin phytotoxins by the Alba protein from Klebsiella oxytoca

Article Abstract:

The albA gene from Klebsiella oxytoca encodes a protein which inactivates albicidin through heat-reversible binding. Albicidin ligand binding to a recombinant AlbA protein, purified by a glutathione S-transferase gene fusion system, is an almost instant and saturable reaction. Kinetic and stoichiometric studies of the binding reaction showed the presence of one high affinity binding site with a dissociation constant of 6.4 x 10(super -8) M. AlbA may be a useful affinity matrix for selective purification of albicidin antibiotics.

Author: Zhang, Lianhui, Birch, Robert G., Xu, Jinling
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Carrier proteins, Transport proteins, Klebsiella

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Subjects list: Antibiotics, Genetic aspects
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