Rat endothelin-converting enzyme-1 forms a dimer through Cys412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11

Biochemical Journal

Volumn 315, Issue 3, 1996, Pages 863-867

  Shimada, Kohei ^a   Takahashi, Masaaki ^a   Turner, Anthony J ^b   Tanzawa, Kazuhiko ^a  

^a DAIICHI SANKYO CO   (Japan)

^b UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; ENDOTHELIN; ENDOTHELIN CONVERTING ENZYME; MEMBRANE METALLOENDOPEPTIDASE; MUTANT PROTEIN; ZINC;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; METAL BINDING; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; RAT; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ENDOPEPTIDASES; BINDING SITES; CATALYSIS; CELL LINE; CYSTEINE; ENDOTHELINS; KINETICS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEPRILYSIN; POINT MUTATION; PROTEIN CONFORMATION; RATS; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 0029997473     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3150863     Document Type: Article

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