| http://purl.uniprot.org/citations/12890666 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12890666 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12890666 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12890666 | http://www.w3.org/2000/01/rdf-schema#comment | "Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in clavulanic acid biosynthesis. The catalytic cycles of CarA and beta-LS mediate substrate adenylation followed by beta-lactamization via a tetrahedral intermediate or transition state. Another member of this family of ATP/Mg2+-dependent enzymes, asparagine synthetase (AS-B), catalyzes intermolecular, rather than intramolecular, amide bond formation in asparagine biosynthesis. The crystal structures of apo-CarA and CarA complexed with the substrate (2S,5S)-5-carboxymethylproline (CMPr), ATP analog alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP), and a single Mg2+ ion have been determined. CarA forms a tetramer. Each monomer resembles beta-LS and AS-B in overall fold, but key differences are observed. The N-terminal domain lacks the glutaminase active site found in AS-B, and an extended loop region not observed in beta-LS or AS-B is present. Comparison of the C-terminal synthetase active site to that in beta-LS reveals that the ATP binding site is highly conserved. By contrast, variations in the substrate binding pocket reflect the different substrates of the two enzymes. The Mg2+ coordination is also different. Several key residues in the active site are conserved between CarA and beta-LS, supporting proposed roles in beta-lactam formation. These data provide further insight into the structures of this class of enzymes and suggest that CarA might be a versatile target for protein engineering experiments aimed at developing improved production methods and new carbapenem antibiotics."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m307901200"xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m307901200"xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Rosenzweig A.C."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Rosenzweig A.C."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Townsend C.A."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Townsend C.A."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Miller M.T."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Miller M.T."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Gerratana B."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Gerratana B."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Stapon A."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/author | "Stapon A."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/pages | "40996-41002"xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/pages | "40996-41002"xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/title | "Crystal structure of carbapenam synthetase (CarA)."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/title | "Crystal structure of carbapenam synthetase (CarA)."xsd:string |
| http://purl.uniprot.org/citations/12890666 | http://purl.uniprot.org/core/volume | "278"xsd:string |