A novel bifunctional peptidic aspartic protease inhibitor inhibits chitinase A from Serratia marcescens: Kinetic analysis of inhibition and binding affinity

Biochimica et Biophysica Acta - General Subjects

Volumn 1800, Issue 5, 2010, Pages 526-536

  Kumar, Ajit ^a,b   Rao, Mala ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

^b DURBAN UNIVERSITY OF TECHNOLOGY   (South Africa)

Author keywords

Aspartic protease inhibitor; Bacillus licheniformis; Chitinase A; Enzyme kinetics; Slow tight binding inhibition

Indexed keywords

4 NITROPHENYL N,N' DIACETYL BETA CHITOBIOSIDE; ASPARTIC PROTEINASE INHIBITOR; BACTERIAL ENZYME; CARBOXYL GROUP; CHITINASE A; CHROMOGENIC SUBSTRATE; ISOINDOLE DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS LICHENIFORMIS; BINDING AFFINITY; CHEMICAL MODIFICATION; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION; DRUG ISOLATION; DRUG SCREENING; ENZYME ACTIVE SITE; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SERRATIA MARCESCENS;

ASPARTIC ACID PROTEASES; BACILLUS; BACTERIAL PROTEINS; CHITINASE; PEPTIDES; PROTEASE INHIBITORS; PROTEIN BINDING; SERRATIA MARCESCENS;

BACILLUS LICHENIFORMIS; SERRATIA MARCESCENS;

EID: 77950367710     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.01.014     Document Type: Article

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