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http://purl.uniprot.org/citations/7608066http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7608066http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7608066http://www.w3.org/2000/01/rdf-schema#comment"The enzyme activities responsible for carboxylation reactions in cell extracts of the gastric pathogen Helicobacter pylori have been studied by H14CO3-fixation and spectrophotometric assays. Acetyl coenzyme A carboxylase (EC 6.4.1.2) and malic enzyme (EC 1.1.1.40) activities were detected, whereas pyruvate carboxylase (EC 6.4.1.1), phosphoenolpyruvate carboxylase (EC 4.1.3.1) and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) activities were absent. However, a pyruvate-dependent, ATP-independent, and avidin-insensitive H14CO3-fixation activity, which was shown to be due to the isotope exchange reaction of pyruvate:flavodoxin oxidoreductase (EC 1.2.7.1), was present. The purified enzyme is composed of four subunits of 47, 36, 24, and 14 kDa. N-terminal sequence analysis showed that this enzyme is related to a recently recognized group of four-subunit pyruvate:ferredoxin oxidoreductases previously known only from hyperthermophiles. This enzyme from H. pylori was found to mediate the reduction of a number of artificial electron acceptors in addition to a flavodoxin isolated from H. pylori extracts, which is likely to be the in vivo electron acceptor. Indirect evidence that the enzyme is capable of in vitro reduction of the anti-H. pylori drug metronidazole was also obtained."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.org/dc/terms/identifier"doi:10.1128/jb.177.14.3953-3959.1995"xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Chalk P.A."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Chalk P.A."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Clayton C.L."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Clayton C.L."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Kelly D.J."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Kelly D.J."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Hughes N.J."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/author"Hughes N.J."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/name"J Bacteriol"xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/pages"3953-3959"xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/pages"3953-3959"xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/title"Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/title"Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori."xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/volume"177"xsd:string
http://purl.uniprot.org/citations/7608066http://purl.uniprot.org/core/volume"177"xsd:string
http://purl.uniprot.org/citations/7608066http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7608066
http://purl.uniprot.org/citations/7608066http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7608066
http://purl.uniprot.org/citations/7608066http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7608066