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Volumn 356, Issue , 2012, Pages 209-214

Catalytic mechanism of human UDP-glucose 6-dehydrogenase: In situ proton NMR studies reveal that the C-5 hydrogen of UDP-glucose is not exchanged with bulk water during the enzymatic reaction

(3) Eixelsberger, Thomas a Brecker, Lothar b Nidetzky, Bernd a

a GRAZ UNIVERSITY OF TECHNOLOGY (Austria)

b UNIVERSITY OF VIENNA (Austria)

Author keywords

Catalytic mechanism; Deuterium incorporation; Thiohemiacetal and thioester intermediates; UDP gluco hexodialdose; UDP glucose dehydrogenase

Indexed keywords

ADDUCT FORMATION; BOVINE LIVER; BULK WATER; CATALYTIC MECHANISMS; CATALYTIC REACTIONS; DETECTION LIMITS; ENZYMATIC REACTION; ENZYMATIC TRANSFORMATION; IN-SITU; KETO-ENOL TAUTOMERISM; PROTON NMR; STEADY STATE; THIOESTERS; UDP-GLUCO-HEXODIALDOSE; UDP-GLUCOSE; UDP-GLUCOSE DEHYDROGENASE; UDP-GLUCURONIC ACID; WILD-TYPE ENZYMES;

CATALYSIS; DEUTERIUM; ENZYMES; HYDROGEN; OXIDATION; PROTONS;

GLUCOSE;

DEUTERIUM; THIOESTER; URIDINE DIPHOSPHATE GLUCOSE; URIDINE DIPHOSPHATE GLUCOSE DEHYDROGENASE; WATER;

CATALYSIS; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME MECHANISM; GLUCOSE OXIDATION; HUMAN; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; WILD TYPE;

BIOCATALYSIS; DEUTERIUM; ESCHERICHIA COLI; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTATION; NAD; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTONS; RECOMBINANT PROTEINS; STEREOISOMERISM; URIDINE DIPHOSPHATE GLUCOSE; URIDINE DIPHOSPHATE GLUCOSE DEHYDROGENASE; URIDINE DIPHOSPHATE GLUCURONIC ACID; WATER;

BOVINAE;

EID: 84862326825 PISSN: 00086215 EISSN: 1873426X Source Type: Journal
DOI: 10.1016/j.carres.2012.03.028 Document Type: Conference Paper

Times cited : (6)

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