A new model for vitamin K-dependent carboxylation: The catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 38, 2004, Pages 13732-13737

  Rishavy, Mark A ^a   Pudota, B Nirmala ^a   Hallgren, Kevin W ^a   Qian, Wen ^a   Yakubenko, Anna V ^a   Song, Jee Hyeon ^a   Runge, Kurt W ^a   Berkner, Kathleen L ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINE; BLOOD CLOTTING FACTOR 9; CARBON 14; CARBOXYLASE; CYSTEINE; GLUTAMIC ACID; HYDROQUINONE; N ETHYLMALEIMIDE; SERINE; VITAMIN K GROUP;

AMINO ACID SUBSTITUTION; APOPTOSIS; ARTICLE; CALCIUM HOMEOSTASIS; CARBOXYLATION; CATALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; HEMOSTASIS; IONIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTON TRANSPORT;

AMINES; ANIMALS; BACULOVIRIDAE; CARBON-CARBON LIGASES; CATALYSIS; CELL LINE; CYSTEINE; CYSTINE; GENETIC VECTORS; HYDROQUINONES; INSECTS; MICROSOMES; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; VITAMIN K;

EID: 4644243445     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0404989101     Document Type: Article

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