The energetics of intramolecular reactions and enzyme catalysis.

M. I. Page

Research output: Contribution to journalReview article

33 Citations (Scopus)

Abstract

The relative rates of reactions should always be examined by an awareness of differential effects. The magnitude and variation of the relative rates of intramolecular reactions can be rationalized by the differences in entropy and strain energy. The relative rates of enzyme-catalysed reactions are sometimes due to groundstate effects. The beta-lactamase-catalysed hydrolysis of beta-lactam antibiotics may require a unique disposition of catalytic groups owing to an unusual process of bond fission in the four membered ring.

LanguageEnglish
Pages149-156
Number of pages8
JournalPhilosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume332
Issue number1263
DOIs
Publication statusPublished - 29 May 1991

Fingerprint

beta-lactam antibiotics
beta-lactamase
enzymatic reactions
beta-Lactams
Entropy
beta-Lactamases
entropy
Strain energy
Catalysis
catalytic activity
Hydrolysis
hydrolysis
Anti-Bacterial Agents
energy
Enzymes
enzymes

Cite this

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The energetics of intramolecular reactions and enzyme catalysis. / Page, M. I.

In: Philosophical transactions of the Royal Society of London. Series B, Biological sciences, Vol. 332, No. 1263, 29.05.1991, p. 149-156.

Research output: Contribution to journalReview article

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