| http://purl.uniprot.org/citations/9497318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9497318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9497318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/9497318 | http://www.w3.org/2000/01/rdf-schema#comment | "The biosynthesis of ansamycin antibiotics, like rifamycin B, involves formation of 3-amino-5-hydroxybenzoic acid (AHBA) by a novel variant of the shikimate pathway. AHBA then serves as the starter unit for the assembly of a polyketide which eventually links back to the amino group of AHBA to form the macrolactam ring. The terminal enzyme of AHBA formation, which catalyzes the aromatization of 5-deoxy-5-amino-3-dehydroshikimic acid, has been purified to homogeneity from Amycolatopsis mediterranei, the encoding gene has been cloned, sequenced, and overexpressed in Escherichia coli. The recombinant enzyme, a (His)6 fusion protein, as well as the native one, are dimers containing one molecule of pyridoxal phosphate per subunit. Mechanistic studies showed that the enzyme-bound pyridoxal phosphate forms a Schiff's base with the amino group of 5-deoxy-5-amino-3-dehydroshikimic acid and catalyzes both an alpha, beta-dehydration and a stereospecific 1,4-enolization of the substrate. Inactivation of the gene encoding AHBA synthase in the A. mediterranei genome results in loss of rifamycin formation; production of the antibiotic is restored when the mutant is supplemented with AHBA."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.11.6030"xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.11.6030"xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Handa S."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Handa S."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Floss H.G."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Floss H.G."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Yu T.W."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Yu T.W."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Kim C.G."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Kim C.G."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Fryhle C.B."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/author | "Fryhle C.B."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/pages | "6030-6040"xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/pages | "6030-6040"xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/title | "3-amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/title | "3-amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics."xsd:string |
| http://purl.uniprot.org/citations/9497318 | http://purl.uniprot.org/core/volume | "273"xsd:string |