Molecular ruler of tripeptidylpeptidase II: Mechanistic principle of exopeptidase selectivity

Biochemical and Biophysical Research Communications

Volumn 414, Issue 1, 2011, Pages 209-214

  Peters, Jürgen ^a   Schönegge, Anne Marie ^a   Rockel, Beate ^a   Baumeister, Wolfgang ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Aminotripeptidase; Double Glu motif; Kinetic study; Molecular ruler; Tripeptidylpeptidase II

Indexed keywords

EXOPEPTIDASE; MUTANT PROTEIN; PROTEINASE; TRIPEPTIDYL PEPTIDASE II; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; MUTATION; PRIORITY JOURNAL; PROTEIN MOTIF; SEQUENCE ALIGNMENT; WILD TYPE;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; ANIMALS; DIPEPTIDYL-PEPTIDASES AND TRIPEPTIDYL-PEPTIDASES; DROSOPHILA MELANOGASTER; GLUTAMIC ACID; KINETICS; POINT MUTATION; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

DROSOPHILA MELANOGASTER;

EID: 80054089021     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.09.058     Document Type: Article

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