This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Marçal, D. Articles by Enguita, F. J. PubMed PubMed Citation Articles by Marçal, D. Articles by Enguita, F. J.

 Previous Article  |  Next Article 

J. Bacteriol. doi:10.1128/JB.01077-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

1,3 propanediol-dehydrogenase from Klebsiella pneumoniae : decameric quaternary structure and possible subunit cooperativity

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal; Unidade de Biologia Celular, Instituto de Medicina Molecular, Universidade de Lisboa, 1649-028 Lisboa, Portugal

^* To whom correspondence should be addressed. Email: fenguita{at}fm.ul.pt.

	Abstract

K. pneumoniae is a nosocomial pathogen frequently isolated from opportunistic infections specially in clinical environments. In spite of its potential pathogenicity, this microorganism has several metabolic potentials that could be used in biotechnology applications. K. pneumoniae is able to metabolize glycerol as a sole source of carbon and energy. 1,3-propanediol dehydrogenase is the core of the metabolic pathway for the use of glycerol. We have determined the crystallographic structure of 1,3-propanediol dehydrogenase, a type III Fe-NAD dependent alcohol dehydrogenase, at 2.7 Å resolution. The structure of the enzyme monomer is closely related to that of other alcohol dehydrogenases. The overall arrangement of the enzyme showed a decameric structure, formed by a pentamer of dimers, which is the catalytic form of the enzyme. Dimers are associated by strong ionic interactions that are responsible for the highly stable in vivo packing of the enzyme. Kinetic properties of the enzyme as determined in the article would suggest that this decameric arrangement is related with the cooperativity between monomers.