Subsites of trypsin active site favor catalysis or substrate binding

Biochemical and Biophysical Research Communications

Volumn 290, Issue 1, 2002, Pages 494-497

  Marana, S R ^a   Lopes, A R ^a   Ferreira, C ^a   Terra, Walter R ^a   Juliano, L ^b   Juliano, M A ^b  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Activation energy; Binding energy; Catalysis; Periplaneta americana; Subsite role; Substrate specificity; Transition state; Trypsin

Indexed keywords

ENZYME; OLIGOPEPTIDE; TRYPSIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING KINETICS; BINDING SITE; CATALYSIS; CHEMICAL REACTION; ENZYME BINDING; HYDROLYSIS; PREDICTION; PRIORITY JOURNAL; REACTION ANALYSIS;

PERIPLANETA; PERIPLANETA AMERICANA;

EID: 0036295709     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.6172     Document Type: Article

References (8)

1. Efficiency and evolution of enzyme catalysis
2. Direct demonstration of the catalytic role of binding interaction in an enzymatic reaction
3. Insect digestive enzymes: Properties, compartmentalization and function
4. Improved silver staining of plant proteins, RNA and DNA in polyacrilamide gels
5. Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides
6. Intramolecular quenched fluorogenic peptide substrate for human renin