Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1

Alanine racemases are ubiquitous, almost uniquely prokaryotic enzymes catalyzing the racemization between l- and d-alanine. The requirement for d-alanine as a necessary component of the bacterial cell wall makes this class of enzymes a logical target for the development of novel antibiotics. In an e...

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Bibliographic Details
Published in:Current microbiology 2000-10, Vol.41 (4), p.290-294
Main Authors: STRYCH, Ulrich, HUANG, Hung-Chung, KRAUSE, Kurt L, BENEDIK, Michael J
Format: Article
Language:English
Subjects:
Alanine Racemase - biosynthesis
Alanine Racemase - genetics
alrPA gene
Amino Acid Sequence
Bacterial Proteins - biosynthesis
Bacterial Proteins - isolation & purification
Bacteriology
Biological and medical sciences
Cloning, Molecular
Crystallization
dadXPA gene
Escherichia coli
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Metabolism. Enzymes
Microbiology
Molecular Sequence Data
Pseudomonas aeruginosa
Pseudomonas aeruginosa - enzymology
Pseudomonas aeruginosa - genetics
Recombinant Proteins - biosynthesis
Sequence Alignment
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Summary:Alanine racemases are ubiquitous, almost uniquely prokaryotic enzymes catalyzing the racemization between l- and d-alanine. The requirement for d-alanine as a necessary component of the bacterial cell wall makes this class of enzymes a logical target for the development of novel antibiotics. In an effort to better understand the structure and mechanism of these enzymes, we have cloned the two independent alanine racemases from Pseudomonas aeruginosa, an important opportunistic bacterial pathogen of humans and animals. The dadX(PA) and alr(PA) genes have been sequenced, overexpressed, and their activity was demonstrated by complementing d-alanine auxotrophs of Escherichia coli. Both gene products were purified to electrophoretic homogeneity, the enzymes were characterized biochemically, and preliminary crystals were obtained.
ISSN:0343-8651
1432-0991
DOI:10.1007/s002840010136