Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state

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

Volumn 94, Issue 17, 1997, Pages 9069-9074

  Sugiura, Isamu ^a,c   Furie, Bruce ^a   Walsh, Christopher T ^b   Furie, Barbara C ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Vitamin K 2,3 epoxide; carboxyglutamic acid

Indexed keywords

GLUTAMIC ACID; PEPTIDE; VITAMIN K DEPENDENT CARBOXYLASE;

ANIMAL CELL; ARTICLE; CARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; EPOXIDATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTHROMBIN TIME; SEQUENCE HOMOLOGY; STEM CELL;

1-CARBOXYGLUTAMIC ACID; AMINO ACID SEQUENCE; ANIMALS; CARBON-CARBON LIGASES; CATTLE; ENZYME ACTIVATION; GLUTAMIC ACID; HUMANS; LIGASES; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PEPTIDES; SUBSTRATE SPECIFICITY;

ANIMALIA; BOVINAE;

EID: 0030741381     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.17.9069     Document Type: Article

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