Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase

Journal of Biological Chemistry

Volumn 283, Issue 29, 2008, Pages 20299-20308

  Belyaeva, Olga V ^a   Johnson, Mary P ^a   Kedishvili, Natalia Y ^a,b  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b 440B Kaul Genetics Bldg ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; ANIMAL CELL CULTURE; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; NUCLEIC ACIDS; OXIDATION; RNA; SUBSTRATES;

BINDING PROTEINS; COFACTOR; HIGH AFFINITIES; HUMAN CELLS; HUMAN ENZYMES; HUMAN RETINOLS; KINETIC ANALYSES; OXIDATIVE ENZYMES; OXIDOREDUCTASES; PHYSIOLOGICAL ROLES; RETINOIC ACIDS; RETINOID; RETINOL DEHYDROGENASES; SUBSTRATE SPECIFICITIES;

ENZYMES;

CELLULAR RETINOL BINDING PROTEIN; CELLULAR RETINOL BINDING PROTEIN 1; HUMAN RETINOL DEHYDROGENASE 10; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; RETINAL; RETINOIC ACID; RETINOL; RETINOL DEHYDROGENASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; ALCOHOL DEHYDROGENASE; TRANS RETINOL DEHYDROGENASE; TRANS-RETINOL DEHYDROGENASE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; EMBRYO; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; AMINO ACID SEQUENCE; ANIMAL; ARMYWORM; CELL LINE; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; DOWN REGULATION; GENE EXPRESSION; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL SURVIVAL; CONSERVED SEQUENCE; DOWN-REGULATION; GENE EXPRESSION; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RETINALDEHYDE; RNA, SMALL INTERFERING; SEQUENCE ALIGNMENT; SPODOPTERA; SUBSTRATE SPECIFICITY; VITAMIN A;

EID: 50649118622     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M800019200     Document Type: Article

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