Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family.

Détails

ID Serval
serval:BIB_8EC557E41183
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family.
Périodique
The Journal of biological chemistry
Auteur(s)
Corthésy-Theulaz I.E., Bergonzelli G.E., Henry H., Bachmann D., Schorderet D.F., Blum A.L., Ornston L.N.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
1997
Peer-reviewed
Oui
Volume
272
Numéro
41
Pages
25659-67
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Résumé
Sequencing of a fragment of Helicobacter pylori genome led to the identification of two open reading frames showing striking homology with Coenzyme A (CoA) transferases, enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. The genes were present in all H. pylori strains tested by polymerase chain reaction or slot blotting but not in Campylobacter jejuni. Genes for the putative A and B subunits of H. pylori CoA-transferase were introduced into the bacterial expression vector pKK223-3 and expressed in Escherichia coli JM105 cells. Amino acid sequence comparisons, combined with measurements of enzyme activities using different CoA donors and acceptors, identified the H. pylori CoA-transferase as a succinyl CoA:acetoacetate CoA-transferase. This activity was consistently observed in different H. pylori strains. Antibodies raised against either recombinant A or B subunits recognized two distinct subunits of Mr approximately 26,000 and 24, 000 that are both necessary for H. pylori CoA-transferase function. The lack of alpha-ketoglutarate dehydrogenase and of succinyl CoA synthetase activities indicates that the generation of succinyl CoA is not mediated by the tricarboxylic acid cycle in H. pylori. We postulate the existence of an alternative pathway where the CoA-transferase is essential for energy metabolism.
Mots-clé
Acyl Coenzyme A, Amino Acid Sequence, Base Sequence, Binding Sites, Campylobacter jejuni, Cloning, Molecular, Coenzyme A-Transferases, DNA, Bacterial, Escherichia coli, Gene Expression, Helicobacter pylori, Humans, Models, Chemical, Molecular Sequence Data, Molecular Weight, Polymerase Chain Reaction
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/01/2008 13:58
Dernière modification de la notice
20/08/2019 15:52
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