pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)

FEBS Letters

Volumn 545, Issue 2-3, 2003, Pages 224-228

  Sigman, Jeffrey A ^a   Edwards, Sarah R ^a   Pabon, Amanda ^b   Glucksman, Marc J ^b   Wolfson, Adele J ^a  

^a WELLESLEY COLLEGE   (United States)

^b ROSALIND FRANKLIN UNIVERSITY OF MEDICINE AND SCIENCE   (United States)

Author keywords

Homology modeling; Metal activation; pH dependence; Thimet oligopeptidase; Transition state stabilization; Tyrosine

Indexed keywords

BASE; ENZYME; HISTIDINE; MUTANT PROTEIN; PHENYLALANINE; THERMOLYSIN; THIMET OLIGOPEPTIDASE; TYROSINE;

ACIDITY; ALKALINITY; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT;

EID: 0037864165     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00548-9     Document Type: Article

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