1,3-Propanediol Dehydrogenase from Klebsiella pneumoniae: Decameric Quaternary Structure and Possible Subunit Cooperativity

被引：57

作者：

Marcal, David ^{[2
]}

Rego, Ana Toste ^{[2
]}

Carrondo, Maria Armenia ^{[2
]}

Enguita, Francisco J. ^{[1
,2
]}

机构：

[1] Univ Lisbon, Inst Mol Med, Unidade Biol Celular, P-1649028 Lisbon, Portugal

[2] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2781901 Oeiras, Portugal

来源：

JOURNAL OF BACTERIOLOGY | 2009年 / 191卷 / 04期

关键词：

GLYCEROL DISSIMILATION; METHANOL DEHYDROGENASE; MICROBIAL-PRODUCTION; CRYSTAL-STRUCTURE; PROTEIN; CRYSTALLOGRAPHY; PURIFICATION; EXPRESSION; DIVERSITY; MOLSURFER;

D O I：

10.1128/JB.01077-08

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Klebsiella pneumoniae is a nosocomial pathogen frequently isolated from opportunistic infections, especially 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-angstrom 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 to the cooperativity between monomers.

引用

页码：1143 / 1151

页数：9

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