Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation

Biochemistry

Volumn 45, Issue 44, 2006, Pages 13239-13248

  Rishavy, Mark A ^a   Hallgren, Kevin W ^a   Yakubenko, Anna V ^a   Shtofman, Rebecca L ^a   Runge, Kurt W ^a   Berkner, Kathleen L ^a  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CARBOXYLATION; CATALYSIS; ENZYME KINETICS; MUTAGENESIS; VITAMINS;

CARBOXYLASE; CATALYTIC BASE; MUTANTS; VITAMIN K;

ENZYMES;

AMINE; HYDROQUINONE; VITAMIN K DEPENDENT CARBOXYLASE; VITAMIN K GROUP;

AMINO ACID SEQUENCE; ARTICLE; BACULOVIRUS EXPRESSION SYSTEM; BIOINFORMATICS; CARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; EPOXIDATION; HYDROPHOBICITY; MUTATIONAL ANALYSIS; PH; PKA; PRIORITY JOURNAL; WESTERN BLOTTING; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CARBON-CARBON LIGASES; CARBOXYLIC ACIDS; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS; SEQUENCE HOMOLOGY, AMINO ACID; VITAMIN K 2;

EID: 33750709274     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0609523     Document Type: Article

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