KOPS - Das Institutionelle Repositorium der Universität Konstanz

Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia

Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:c8698d72469164673146680782471348

LAUE, Heike, Alasdair M. COOK, 2000. Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia. In: European Journal of Biochemistry. 267(23), pp. 6841-6848. eISSN 0014-2956. Available under: doi: 10.1046/j.1432-1033.2000.01782.x

@article{Laue2000Bioch-7868, title={Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia}, year={2000}, doi={10.1046/j.1432-1033.2000.01782.x}, number={23}, volume={267}, journal={European Journal of Biochemistry}, pages={6841--6848}, author={Laue, Heike and Cook, Alasdair M.} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7868"> <dcterms:abstract xml:lang="eng">Bilophila wadsworthia RZATAU is a Gram-negative bacterium which converts the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and sulfide in an anaerobic respiration. Taurine:pyruvate aminotransferase (Tpa) catalyses the initial metabolic reaction yielding alanine and sulfoacetaldehyde. We purified Tpa 72-fold to apparent homogeneity with an overall yield of 89%. The purified enzyme did not require addition of pyridoxal 5'-phosphate, but highly active enzyme was only obtained by addition of pyridoxal 5'-phosphate to all buffers during purification. SDS/PAGE revealed a single protein band with a molecular mass of 51 kDa. The apparent molecular mass of the native enzyme was 197 kDa as determined by gel filtration, which indicates a homotetrameric structure. The kinetic constants for taurine were: Km = 7.1 mm, Vmax = 1.20 nmol·s-1, and for pyruvate: Km = 0.82 mm, Vmax = 0.17 nmol·s-1. The purified enzyme was able to transaminate hypotaurine (2-aminosulfinate), taurine, beta-alanine and with low activity cysteine and 3-aminopropanesulfonate. In addition to pyruvate, 2-ketobutyrate and oxaloacetate were utilized as amino group acceptors. We have sequenced the encoding gene (tpa). It encoded a 50-kDa peptide, which revealed 33% identity to diaminopelargonate aminotransferase from Bacillus subtilis.</dcterms:abstract> <dc:language>eng</dc:language> <dc:contributor>Cook, Alasdair M.</dc:contributor> <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 267 (2000), 23, pp. 6841-6848</dcterms:bibliographicCitation> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7868/1/Biochemical.pdf"/> <dcterms:issued>2000</dcterms:issued> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:09Z</dc:date> <dc:creator>Cook, Alasdair M.</dc:creator> <dcterms:title>Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia</dcterms:title> <dc:contributor>Laue, Heike</dc:contributor> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7868/1/Biochemical.pdf"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7868"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:09Z</dcterms:available> <dc:creator>Laue, Heike</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:format>application/pdf</dc:format> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Biochemical.pdf 137

Das Dokument erscheint in:

deposit-license Solange nicht anders angezeigt, wird die Lizenz wie folgt beschrieben: deposit-license

KOPS Suche


Stöbern

Mein Benutzerkonto