Evidence by site-directed mutagenesis that Arginine 203 of thermolysin and arginine 717 of neprilysin (neutral endopeptidase) play equivalent critical roles in substrate hydrolysis and inhibitor binding

Biochemistry

Volumn 36, Issue 45, 1997, Pages 13938-13945

  Marie Claire, Cynthia ^a   Ruffet, Emmanuel ^a   Antonczak, Serge ^a   Beaumont, Ann ^a   O'Donohue, Michael ^a,b   Roques, Bernard P ^a   Fournié Zaluski, Marie Claude ^a  

^a Laboratoire de Pharmacochimie   (France)

^b U Physchim Biotech des Polymeres   (France)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE METALLOENDOPEPTIDASE; THERMOLYSIN;

AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME INHIBITION; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ARGININE; BACILLUS SUBTILIS; BINDING, COMPETITIVE; DNA, COMPLEMENTARY; GLYCOPEPTIDES; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEPRILYSIN; PROTEASE INHIBITORS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMOLYSIN; THIORPHAN;

BACTERIA (MICROORGANISMS); FELIS CATUS; MAMMALIA;

EID: 0030656495     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9712495     Document Type: Article

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