Structural and kinetic evidence that catalytic reaction of human UPD-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates

Journal of Biological Chemistry

Volumn 287, Issue 3, 2012, Pages 2119-2129

  Egger, Sigrid ^a,c   Chaikuad, Apirat ^b   Klimacek, Mario ^a   Kavanagh, Kathryn L ^b   Oppermann, Udo ^b   Nidetzky, Bernd ^a,c  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c AUSTRIAN CENTRE OF INDUSTRIAL BIOTECHNOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL OXIDATION; CATALYTIC BASE; CATALYTIC CYCLES; CATALYTIC MECHANISMS; CATALYTIC NUCLEOPHILES; CATALYTIC REACTIONS; ENZYMATIC MECHANISMS; GENERAL BASE; HYDRIDE TRANSFERS; KINETIC EVIDENCE; OXYANIONS; PRIMARY ALCOHOLS; RATE LIMITING; STEADY STATE; THIOESTERS; UDP-GLUCOSE; UDP-GLUCURONIC ACID;

ALDEHYDES; BIOCHEMISTRY; CATALYSIS; CATALYTIC OXIDATION; ENZYMES; GLUCOSE; HYDROLYSIS; NUCLEOPHILES; OXIDATION; POSITIVE IONS; QUANTUM CHEMISTRY; STABILIZATION;

REACTION INTERMEDIATES;

ACETAL; ASPARAGINE; BRONSTED BASE; CYSTEINE; GLUTAMINE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOESTER; THIOHEMIACETAL; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE DEHYDROGENASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SYNTHESIS; HUMAN; HYDROLYSIS; NUCLEOPHILICITY; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; STEADY STATE;

AMINO ACID SUBSTITUTION; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; KINETICS; MUTATION, MISSENSE; NAD; OXIDATION-REDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; URIDINE DIPHOSPHATE GLUCOSE; URIDINE DIPHOSPHATE GLUCOSE DEHYDROGENASE;

EID: 84855857694     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.313015     Document Type: Article

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