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Volumn 441, Issue 1, 2005, Pages 25-34

Characterization of thimet- and neurolysin-like activities in Escherichia coli M3A peptidases and description of a specific substrate

(5) Paschoalin, Thaysa a Carmona, Adriana K a Oliveira, Vitor a Juliano, Luiz a Travassos, Luiz R a

a FEDERAL UNIVERSITY OF SÃO PAULO (Brazil)

Author keywords

Co purification; Dipeptidyl dipeptidase (Dcp); Escherichia coli; Expression vector; M3A subfamily; Neurolysin; Oligopeptidase A (OpdA); Recombinant protein; Specific substrate; Thimet oligopeptidase

Indexed keywords

AMINO ACID DERIVATIVE; BACTERIUM LYSATE; BRADYKININ; DIPEPTIDYL CARBOXYPEPTIDASE; FLUORESCENT DYE; LEUPEPTIN; NEUROLYSIN; NEUROTENSIN; OLIGOPEPTIDASE A; PEPTIDASE; PEPTIDE; PEPTIDE DERIVATIVE; PHORATE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BACTERIOLYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GEL FILTRATION; GENETIC CODE; GENOME; HYDROLYSIS; MOLECULAR CLONING; MOLECULAR RECOGNITION; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; BRADYKININ; ENZYME ACTIVATION; ESCHERICHIA COLI; KINETICS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NEUROTENSIN; PEPTIDE HYDROLASES; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; MAMMALIA;

EID: 23944455859 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/j.abb.2005.06.011 Document Type: Article

Times cited : (8)

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