Residue 225 determines the Na+-induced allosteric regulation of catalytic activity in serine proteases

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

Volumn 93, Issue 20, 1996, Pages 10653-10656

  Dang, Quoc D ^a   Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

allostery; blood coagulation; complement; molecular evolution

Indexed keywords

SERINE PROTEINASE; SODIUM ION; THROMBIN; TRYPSIN;

ALLOSTERISM; ARTICLE; BINDING SITE; BLOOD CLOTTING; CATALYSIS; COMPLEMENT SYSTEM; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; EVOLUTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; STRUCTURE ACTIVITY RELATION;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; BINDING SITES; CATIONS, MONOVALENT; CELL-FREE SYSTEM; HUMANS; MODELS, MOLECULAR; SERINE ENDOPEPTIDASES; SODIUM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THROMBIN; TYROSINE;

BACTERIA (MICROORGANISMS); VERTEBRATA;

EID: 0029785840     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.20.10653     Document Type: Article

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