Unexpected crucial role of residue 225 in serine proteases

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

Volumn 96, Issue 5, 1999, Pages 1852-1857

  Guinto, Enriqueta R ^a   Caccia, Sonia ^a   Rose, Thierry ^a   Fütterer, Klaus ^a   Waksman, Gabriel ^a   Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Complement; Molecular evolution; Thrombin; Water

Indexed keywords

AQUAPORIN; MUTANT PROTEIN; PHENYLALANINE; PROLINE; SERINE; SERINE PROTEINASE; THROMBIN; TYROSINE;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME CONFORMATION; MOLECULAR EVOLUTION; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BLOOD COAGULATION FACTORS; CHYMOTRYPSIN; COMPLEMENT SYSTEM PROTEINS; CRYSTALLOGRAPHY, X-RAY; DATABASES; EVOLUTION, MOLECULAR; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROLINE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; THROMBIN; TRYPSIN; TYROSINE;

VERTEBRATA;

EID: 0033515039     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.5.1852     Document Type: Article

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