Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates

Biological Chemistry

Volumn 393, Issue 7, 2012, Pages 631-640

  Petrera, Agnese ^a   Amstutz, Beat ^a   Gioia, Magda ^b,c   Hähnlein, Janine ^a   Baici, Antonio ^a   Selchow, Petra ^a   Ferraris, Davide M ^d   Rizzi, Menico ^d   Sbardella, Diego ^b,c   Marini, Stefano ^b,c   Coletta, Massimo ^b,c   Sander, Peter ^a,e  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

^c Interuniversity Consortium for Research on Chemistry of Metals in Biological Systems   (Italy)

^d UNIVERSITY OF EASTERN PIEDMONT   (Italy)

^e Nationales Zentrum fur Mykobakterien   (Switzerland)

Author keywords

Drug development; Enzyme kinetics; Metallo peptidase; Mycobacterium tuberculosis; Peptide hormones; Phagosome maturation

Indexed keywords

AMINO ACID; BRADYKININ; ISOLEUCINE; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; NEUROPEPTIDE; NEUROPEPTIDE FF; NEUROTENSIN; PHENYLALANINE; UNCLASSIFIED DRUG; ZINC METALLOPEPTIDASE 1;

ARTICLE; BACTERIAL VIRULENCE; CONTROLLED STUDY; MASS SPECTROMETRY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PH; PHAGOSOME; PRIORITY JOURNAL;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; INDOLES; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; KINETICS; METALLOPROTEASES; MYCOBACTERIUM TUBERCULOSIS; NEUROPEPTIDES; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEOLYSIS; SUBSTANCE P; SUBSTRATE SPECIFICITY; ZINC;

EID: 84867827439     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0106     Document Type: Article

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