http://purl.uniprot.org/citations/3619918 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3619918 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3619918 | http://www.w3.org/2000/01/rdf-schema#comment | "The beta 3 beta 3 (formerly called beta Indianapolis) and beta 1 beta 1 isoenzymes of human alcohol dehydrogenase differ substantially in their catalytic properties. Specifically, the KM value for NAD+ of beta 3 beta 3 is 70 times greater than that of beta 1 beta 1, and the Ki value for NADH is 35 times greater than that of beta 1 beta 1. To identify the structural basis of these catalytic differences, we sequenced regions of the beta 3 subunit and the beta 3 gene. beta 3 differs from beta 1 by the substitution of Cys for Arg-369. Based on x-ray crystallography of horse ADH, Arg-369 should interact with the nicotinamide phosphate moiety of NAD(H). The Cys for Arg-369 substitution would decrease the enzyme's affinity for coenzyme and, thus, account for the observed kinetic differences between beta 3 beta 3 and beta 1 beta 1."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.org/dc/terms/identifier | "doi:10.1016/0006-291x(87)90779-0"xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.org/dc/terms/identifier | "doi:10.1016/0006-291x(87)90779-0"xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Edenberg H.J."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Edenberg H.J."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Bosron W.F."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Bosron W.F."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Burnell J.C."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Burnell J.C."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Carr L.G."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Carr L.G."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Dwulet F.E."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Dwulet F.E."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Li T.-K."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/author | "Li T.-K."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/pages | "1127-1133"xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/pages | "1127-1133"xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/title | "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding."xsd:string |
http://purl.uniprot.org/citations/3619918 | http://purl.uniprot.org/core/title | "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding."xsd:string |