Get paper from

journal cover

Enzyme substrate and inhibitor interactions

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences

Nov 6, 1975

D M Blow, J Michael Smith

Get paper from

Abstract

An enzyme is designed to bind most tightly to a substrate when it is in the transition state of the reaction which the enzyme catalyses. The consequent reduction of the activation energy of the reaction constitutes the catalytic mechanism. The energetic contributions of different featur...read more

Mentioned in this Paper

Models, Structural
Complex (molecular entity)
Tertiary Protein Structure
Enzyme Inhibitor Drugs
Trypsin
Catalysis
Structure-Activity Relationship
Protein Conformation
Site
Hydrogen Bonding

Enzyme substrate and inhibitor interactions

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences

Nov 6, 1975

D M Blow, J Michael Smith

PMID: 1820

DOI: 10.1098/rstb.1975.0072

Abstract

An enzyme is designed to bind most tightly to a substrate when it is in the transition state of the reaction which the enzyme catalyses. The consequent reduction of the activation energy of the reaction constitutes the catalytic mechanism. The energetic contributions of different featur...read more

Mentioned in this Paper

Models, Structural
Complex (molecular entity)
Tertiary Protein Structure
Enzyme Inhibitor Drugs
Trypsin

Related Papers

Get paper from

© 2019 Meta ULC. All rights reserved.
/papers/enzyme-substrate-and-inhibitor/1820