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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/2000/01/rdf-schema#comment | "Spontaneous mutants which acquired the ability to utilize d-allylglycine (d-2-amino-4-pentenoic acid) and dl-cis-crotylglycine (dl-2-amino-cis-4-hexenoic acid) but not l-allylglycine or dl-trans-crotylglycine could be readily isolated from Pseudomonas putida mt-2 (PaM1). Derivative strains of PaM1 putatively cured of the TOL (pWWO) plasmid were incapable of forming mutants able to utilize the amino acids for growth; however, this ability could be regained by conjugative transfer of the TOL (pWWO) plasmid from a wild-type strain of mt-2 or of the TOL (pDK1) plasmid from a related strain of P. putida (HS1), into cured recipients. dl-Allylglycine-grown cells of one spontaneous mutant (PaM1000) extensively oxidized dl-allylglycine and dl-cis-crotylglycine, whereas only a limited oxidation was observed toward l-allylglycine and dl-trans-crotylglycine. Cell extracts prepared from PaM1000 cells contained high levels of 2-keto-4-hydroxyvalerate aldolase and 2-keto-4-pentenoic acid hydratase, the latter enzyme showing higher activity toward 2-keto-cis-4-hexenoic acid than toward the trans isomer. Levels of other enzymes of the TOL degradative pathway, including toluate oxidase, catechol-2,3-oxygenase, 2-hydroxymuconic semialdehyde hydrolase, and 2-hydroxymuconic semialdehyde dehydrogenase, were also found to be elevated after growth on allylglycine. Whole cells of a putative cured strain, PaM3, accumulated 2-keto-4-pentenoic acid from d-allylglycine, which was shown to be rapidly degraded by cell extracts of PaM1000 grown on dl-allylglycine. These same cell extracts were also capable of catalyzing the dehydrogenation of d-but not l-allylglycine and were further found to metabolize the amino acid completely to pyruvate and acetaldehyde. Differential centrifugation of crude cell extracts localized d-allylglycine dehydrogenase activity to membrane fractions. The results are consistent with a catabolic pathway for d-allylglycine and dl-cis-crotylglycine involving the corresponding keto-enoic acids as intermediates, the further metabolism of which is effected by the action of TOL plasmid-encoded enzymes."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.148.1.72-82.1981"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Chapman P.J."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Chapman P.J."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Ribbons D.W."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Ribbons D.W."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Kunz D.A."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/author | "Kunz D.A."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/date | "1981"xsd:gYear |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/date | "1981"xsd:gYear |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/name | "J Bacteriol"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/pages | "72-82"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/pages | "72-82"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/title | "Metabolism of allylglycine and cis-crotylglycine by Pseudomonas putida (arvilla) mt-2 harboring a TOL plasmid."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/title | "Metabolism of allylglycine and cis-crotylglycine by Pseudomonas putida (arvilla) mt-2 harboring a TOL plasmid."xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/volume | "148"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://purl.uniprot.org/core/volume | "148"xsd:string |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7287632 |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7287632 |
| http://purl.uniprot.org/citations/7287632 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7287632 |
| http://purl.uniprot.org/citations/7287632 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7287632 |