Influence of the conformational flexibility on the kinetics and dimerisation process of two Candida rugosa lipase isoenzymes

FEBS Letters

Volumn 501, Issue 1, 2001, Pages 87-91

  Pernas, María A ^a   López, Cristina ^a   Rúa, M Luisa ^a   Hermoso, Juan ^b  

^a UNIVERSITY OF VIGO   (Spain)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

Author keywords

Candida rugosa; Dimerization; Inhibition; Interfacial activation; Kinetic; Lipase; Structure

Indexed keywords

ISOENZYME; LIPASE ISOENZYME; UNCLASSIFIED DRUG; ENZYME INHIBITOR; PARAOXON; TRIACETIN; TRIACYLGLYCEROL LIPASE;

ARTICLE; BINDING AFFINITY; CANDIDA RUGOSA; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; BINDING SITE; CANDIDA; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; DRUG ANTAGONISM; ENZYMOLOGY; GEL CHROMATOGRAPHY; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR WEIGHT; PLIABILITY; PROTEIN QUATERNARY STRUCTURE;

BINDING SITES; CANDIDA; CHROMATOGRAPHY, GEL; DIMERIZATION; ENZYME INHIBITORS; ISOENZYMES; KINETICS; LIPASE; MODELS, MOLECULAR; MOLECULAR WEIGHT; PARAOXON; PLIABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TRIACETIN;

EID: 0035854699     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/S0014-5793(01)02630-8     Document Type: Article

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