Bradykinin analogues with β-amino acid substitutions reveal subtle differences in substrate specificity between the endopeptidases EC 3.4.24. 15 and EC 3.4.24.16

Journal of Peptide Science

Volumn 6, Issue 9, 2000, Pages 440-445

  Lew, Rebecca A ^a   Boulos, Elie ^b   Stewart, Karen M ^b   Perlmutter, Patrick ^c   Harte, Michael F ^c   Bond, Silas ^c   Aguilar, Marie Isabel ^b   Ian Smith, A ^a  

^a BAKER IDI HEART AND DIABETES INSTITUTE   (Australia)

^b Department of Biochemistry and Molecular Biology ^*  (Australia)

^c MONASH UNIVERSITY   (Australia)

Author keywords

amino acid; Bradykinin; Peptidase inhibitor; Zinc metalloendopeptidase

Indexed keywords

ALANINE; BETA AMINO ACID; BRADYKININ DERIVATIVE; GLYCINE; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; PHENYLALANINE; RECOMBINANT PROTEIN; SERINE; THIMET OLIGOPEPTIDASE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; DRUG DEGRADATION; DRUG SYNTHESIS; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; IC 50; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN INTERACTION; STEREOISOMERISM;

ALANINE; AMINO ACID SUBSTITUTION; ANIMAL; BRADYKININ; COMPARATIVE STUDY; DOSE-RESPONSE RELATIONSHIP, DRUG; GLYCINE; HYDROLYSIS; KINETICS; METALLOENDOPEPTIDASES; PEPTIDE FRAGMENTS; RATS; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T;

EID: 0033828631     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/1099-1387(200009)6:9<440::AID-PSC280>3.0.CO;2-K     Document Type: Article

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