DC Field | Value | Language |
---|---|---|
dc.contributor.author | Maurice, Martin St. | ko |
dc.contributor.author | Mera, Paola | ko |
dc.contributor.author | Park, Kiyoung | ko |
dc.contributor.author | Brunold, Thomas C. | ko |
dc.contributor.author | Escalante-Semerena, Jorge C. | ko |
dc.contributor.author | Rayment, Ivan | ko |
dc.date.accessioned | 2015-11-20T10:28:06Z | - |
dc.date.available | 2015-11-20T10:28:06Z | - |
dc.date.created | 2014-08-05 | - |
dc.date.created | 2014-08-05 | - |
dc.date.issued | 2008-05 | - |
dc.identifier.citation | BIOCHEMISTRY, v.47, no.21, pp.5755 - 5766 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10203/201427 | - |
dc.description.abstract | ATP:cob(I)alamin adenosyltransferases (ACAs) catalyze, the transfer of the 5'-deoxyadenosyl moiety from ATP to the upper axial ligand position of cobalamin in the synthesis of coenzyme B-12. For the ACA-catalyzed reaction to proceed, cob(II)alamin must be reduced to cob(I)alamin in the enzyme active site. This reduction is facilitated through the generation of a four-coordinate cob(II)alamin intermediate on the enzyme. We have determined the high-resolution crystal structure of a human-type ACA from Lactobacillus reuteri with a four-coordinate cob(II)alamin bound in the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site. The assembled structures represent snapshots of the steps in the ACA-catalyzed formation of the cobalt-carbon bond of coenzyme B-12. The structures define the corrinoid binding site and provide visual evidence for a base-off, four-coordinate cob(II)alamin intermediate. The complete structural description of ACA-mediated catalysis reveals the molecular features of four-coordinate cob(II)alamin stabilization and provides additional insights into the molecular basis for dysfunction in human patients suffering from methylmalonic aciduria. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | METHYLMALONYL-COA MUTASE | - |
dc.subject | X-RAY-STRUCTURE | - |
dc.subject | SALMONELLA-ENTERICA | - |
dc.subject | ATP-COB(I)ALAMIN ADENOSYLTRANSFERASE | - |
dc.subject | COBALAMIN ADENOSYLTRANSFERASE | - |
dc.subject | ELECTRONIC-PROPERTIES | - |
dc.subject | METHIONINE SYNTHASE | - |
dc.subject | CO2+ COBALAMIN | - |
dc.subject | ATP-CO(I)RRINOID ADENOSYLTRANSFERASE | - |
dc.subject | INITIAL-CHARACTERIZATION | - |
dc.title | Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B-12 is synthesized through a four-coordinate intermediate | - |
dc.type | Article | - |
dc.identifier.wosid | 000256043200009 | - |
dc.identifier.scopusid | 2-s2.0-44349154911 | - |
dc.type.rims | ART | - |
dc.citation.volume | 47 | - |
dc.citation.issue | 21 | - |
dc.citation.beginningpage | 5755 | - |
dc.citation.endingpage | 5766 | - |
dc.citation.publicationname | BIOCHEMISTRY | - |
dc.identifier.doi | 10.1021/bi800132d | - |
dc.contributor.localauthor | Park, Kiyoung | - |
dc.contributor.nonIdAuthor | Maurice, Martin St. | - |
dc.contributor.nonIdAuthor | Mera, Paola | - |
dc.contributor.nonIdAuthor | Brunold, Thomas C. | - |
dc.contributor.nonIdAuthor | Escalante-Semerena, Jorge C. | - |
dc.contributor.nonIdAuthor | Rayment, Ivan | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | METHYLMALONYL-COA MUTASE | - |
dc.subject.keywordPlus | X-RAY-STRUCTURE | - |
dc.subject.keywordPlus | SALMONELLA-ENTERICA | - |
dc.subject.keywordPlus | ATP-COB(I)ALAMIN ADENOSYLTRANSFERASE | - |
dc.subject.keywordPlus | COBALAMIN ADENOSYLTRANSFERASE | - |
dc.subject.keywordPlus | ELECTRONIC-PROPERTIES | - |
dc.subject.keywordPlus | METHIONINE SYNTHASE | - |
dc.subject.keywordPlus | CO2+ COBALAMIN | - |
dc.subject.keywordPlus | ATP-CO(I)RRINOID ADENOSYLTRANSFERASE | - |
dc.subject.keywordPlus | INITIAL-CHARACTERIZATION | - |
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