Deregulation of allosteric response of Lactococcus lactis prolidase and its effects on enzyme activity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 6, 2009, Pages 968-975

  Zhang, Guodong ^a,b   Chen, Jian An ^a   Tanaka, Takuji ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b Faculty of Bioengineering   (China)

Author keywords

Bitterness; Flexible loop; Peptidase; Proline; Protein engineering; Proteolysis

Indexed keywords

ARGININE; HISTIDINE; PROLINE DIPEPTIDASE; SERINE;

ALLOSTERISM; ARTICLE; COMPUTER MODEL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME REGULATION; LACTOCOCCUS LACTIS; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; SUBSTITUTION REACTION;

ALLOSTERIC REGULATION; BASE SEQUENCE; DIPEPTIDASES; DNA PRIMERS; LACTOCOCCUS LACTIS; MODELS, MOLECULAR; SUBSTRATE SPECIFICITY;

LACTOCOCCUS LACTIS;

EID: 67349088481     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.01.008     Document Type: Article

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