Characterization of recombinant prolidase from Lactococcus lactis - Changes in substrate specificity by metal cations, and allosteric behavior of the peptidase

FEBS Journal

Volumn 275, Issue 2, 2008, Pages 271-280

  Yang, Soo I ^a   Tanaka, Takuji ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

Bitterness; Metallopeptidase; Overexpression; PepQ; Proline

Indexed keywords

ARGININE; LEUCINE; MANGANESE; METAL ION; PROLINE; PROLINE DIPEPTIDASE; RECOMBINANT ENZYME; ZINC;

ACIDITY; ALKALINITY; ALLOSTERISM; ARTICLE; BACTERIAL CELL; BACTERIAL GENE; BACTERIAL GROWTH; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE OVEREXPRESSION; LACTOCOCCUS LACTIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL;

ALLOSTERIC REGULATION; BASE SEQUENCE; CATIONS; CLONING, MOLECULAR; DIPEPTIDASES; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LACTOCOCCUS LACTIS; MODELS, MOLECULAR; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; LACTOCOCCUS LACTIS;

EID: 37849015455     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06197.x     Document Type: Article

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