Linked Life Data

11298756

Source:http://linkedlifedata.com/resource/pubmed/id/11298756

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2001-4-12
pubmed:databankReference
pubmed:abstractText
The coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii is subject to suicide inactivation by the natural substrate glycerol during catalysis. We identified dhaF and dhaG as the genes responsible for reactivation of inactivated dehydratase. Northern blot analyses revealed that both genes were expressed during glycerol fermentation. The dhaF gene is transcribed together with the three structural genes coding for glycerol dehydratase (dhaBCE), whereas dhaG is coexpressed with the dhaT gene encoding 1,3-propanediol dehydrogenase. The dhaF and dhaG gene products were copurified to homogeneity from cell-free extracts of a recombinant E. coli strain producing both His6-tagged proteins. Both proteins formed a tight complex with an apparent molecular mass of 150 000 Da. The subunit structure of the native complex is probably alpha2beta2. The factor rapidly reactivated glycerol- or O2-inactivated hologlycerol dehydratase and activated the enzyme-cyanocobalamin complex in the presence of coenzyme B12, ATP, and Mg2+. The DhaF-DhaG complex and DhaF exhibited ATP-hydrolyzing activity, which was not directly linked to the reactivation of dehydratase. The purified DhaF-DhaG complex of C. freundii efficiently cross-activated the enzyme-cyanocobalamin complex and the glycerol-inactivated glycerol dehydratase of Klebsiella pneumoniae. It was not effective with respect to the glycerol dehydratase of Clostridium pasteurianum and to diol dehydratases of enteric bacteria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2369-78
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:11298756-Adenosine Triphosphatases, pubmed-meshheading:11298756-Adenosine Triphosphate, pubmed-meshheading:11298756-Bacterial Proteins, pubmed-meshheading:11298756-Blotting, Northern, pubmed-meshheading:11298756-Blotting, Western, pubmed-meshheading:11298756-Catalysis, pubmed-meshheading:11298756-Cell-Free System, pubmed-meshheading:11298756-Chromatography, Thin Layer, pubmed-meshheading:11298756-Citrobacter freundii, pubmed-meshheading:11298756-Clostridium, pubmed-meshheading:11298756-Cobamides, pubmed-meshheading:11298756-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11298756-Enzyme Activation, pubmed-meshheading:11298756-Escherichia coli, pubmed-meshheading:11298756-Fermentation, pubmed-meshheading:11298756-Glycerol, pubmed-meshheading:11298756-Histidine, pubmed-meshheading:11298756-Hydro-Lyases, pubmed-meshheading:11298756-Hydrolysis, pubmed-meshheading:11298756-Klebsiella pneumoniae, pubmed-meshheading:11298756-Magnesium, pubmed-meshheading:11298756-Models, Genetic, pubmed-meshheading:11298756-Molecular Sequence Data, pubmed-meshheading:11298756-Nucleic Acid Hybridization, pubmed-meshheading:11298756-Protein Binding, pubmed-meshheading:11298756-Recombinant Proteins, pubmed-meshheading:11298756-Time Factors, pubmed-meshheading:11298756-Transcription, Genetic
pubmed:year
2001
pubmed:articleTitle
Identification and expression of the genes and purification and characterization of the gene products involved in reactivation of coenzyme B12-dependent glycerol dehydratase of Citrobacter freundii.
pubmed:affiliation
Abteilung Allgemeine Mikrobiologie, Institut für Mikrobiologie und Genetik der Georg-August-Universität, Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't