Abstract
Since adsorption of the substrate in the active site of an enzyme can occur only if all solvent is squeezed out from between them, any reaction between them takes place in the absence of any intervening solvent--i.e., as it would in the gas phase. Recent work has shown that ionic reactions in the gas phase often differ greatly from analogous processes in solution. Therefore, current interpretations of enzyme reactions in terms of solution chemistry are misguided. The large rates and specificity of enzyme reactions may be due simply to elimination of the solvent. The cleavage of peptides by chymotrypsin and carboxypeptidase A can be interpreted satisfactorily in this way.
Keywords
ChemistryCarboxypeptidaseSolventIonic bondingEnzymeSubstrate (aquarium)ChymotrypsinActive siteEnzyme catalysisGas phaseComputational chemistryCombinatorial chemistryStereochemistryOrganic chemistryTrypsinBiologyIon
Related Publications
Hydrolysis of Biological Peptides by Human Angiotensin-converting Enzyme-related Carboxypeptidase
Human angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a zinc metalloprotease whose closest homolog is angiotensin I-converting enzyme. To begin to elucidate the...
A Novel Angiotensin-Converting Enzyme–Related Carboxypeptidase (ACE2) Converts Angiotensin I to Angiotensin 1-9
Abstract —ACE2, the first known human homologue of angiotensin-converting enzyme (ACE), was identified from 5′ sequencing of a human heart failure ventricle cDNA library. ACE2 h...
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
New protein parameters are reported for the all-atom empirical energy function in the CHARMM program. The parameter evaluation was based on a self-consistent approach designed t...
Hepatocyte growth factor is a preferred <i>in vitro</i> substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
Hepsin is a membrane-anchored, trypsin-like serine protease with prominent expression in the human liver and tumours of the prostate and ovaries. To better understand the biolog...
A High Resolution Structure of an Inhibitor Complex of the Extracellular Nuclease of Staphylococcus aureus
Two isomorphously substituted derivatives of the nuclease-Ca2+-thymidine 3',5'-diphosphate complex have been prepared and used in an x-ray crystallographic study of the molecula...
Publication Info
- Year
- 1985
- Type
- article
- Volume
- 82
- Issue
- 8
- Pages
- 2225-2229
- Citations
- 193
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
193
OpenAlex
Cite This
Michael J. S. Dewar,
Donn M. Storch
(1985).
Alternative view of enzyme reactions..
Proceedings of the National Academy of Sciences
, 82
(8)
, 2225-2229.
https://doi.org/10.1073/pnas.82.8.2225
Identifiers
- DOI
- 10.1073/pnas.82.8.2225