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A classification of enzyme inhibitors

Bioorganic & Medicinal Chemistry Letters, 1992
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
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Thiosemicarbazones as inhibitors of tyrosinase enzyme

Bioorganic & Medicinal Chemistry Letters, 2017
In the search for compounds which may inhibit the development of melanomas, a series of thiosemicarbazones has been investigated as possible inhibitors of the tyrosinase enzyme. The results showed that all the thiosemicarbazones tested exhibited significant inhibitory effects on the enzyme.
Mariana A. Soares   +5 more
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Interactions of enzymes and inhibitors

Journal of Chemical Education, 1967
Examines the kinetics and interactions of enzymes and inhibitors and considers specifically lactic dehydrogenase, dihydrofolic reductase, thymidine phosphorylate, guanase, and xanthine oxidase.
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Plant inhibitors of proteolytic enzymes

Food / Nahrung, 1984
AbstractThe presence of inhibitors of proteinases was stated in many species of plants. There are macropeptides of the molecular weight ranging from 3700 to 8000, often bound to carbohydrates. Potential sources of inhibitors of proteinases are legumes, cereals, potatoes and also some fruits. They are characterized by different activity. „Single‐headed”︁
B. Romanowska, G. Mossor, J. Skupin
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Enzyme substrate and inhibitor interactions

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1975
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.
D. M. Blow, John Maynard Smith
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Converting Enzyme Inhibitors

1990
Converting enzyme (CE; EC 3.4.15.1) is an exopeptidase which catalyzes the hydrolytic removal of carboxyterminal dipeptide residues from polypeptide substrates. This enzyme is involved in blood pressure regulation in a unique manner. First, it catalyzes the conversion of the inactive decapeptide angiotensin I (ANG I) to the octapeptide, angiotensin II (
M.-G. Gruber, T. Unger, P. Gohlke
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Angiotensin-converting enzyme inhibitors

2001
Publisher Summary Angiotensin-converting enzyme (ACE) inhibitors were first studied clinically in the 1970s. ACE inhibitors were discovered by taking advantage of previous basic research on the physiology of sodium, potassium, and water homeostasis and blood pressure regulation, in a reciprocal way ACE have also advanced research in this field, and ...
Arthur A. Patchett, Joël Ménard
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Protein inhibitors of enzymes

Food Chemistry, 1981
Abstract The range of proteins from plants which form reversible stoichiometric protein-protein complexes with enzymes, thus inhibiting their catalytic functions, is surveyed. Details of the biochemistry of the proteinase- and α-amylase inhibitors found in the important food crops such as the cereals, legumes and potatoes are given.
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angiotensin converting enzyme inhibitors

2012
More than 30 years since their discovery, angiotensin-converting enzyme (ACE) inhibitors still represent one of the most commonly prescribed medications for treating hypertension and one of the favored first-line agents, particularly in the presence of high-risk conditions, such as diabetes.
GENTILE, GIORGIO   +4 more
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Biomimetic enzyme inhibitors

2010
Synthetic biomimetic compounds play crucial roles in virtually all aspects of biology and medicine. Their continual development contributes towards understanding and manipulating the normal action of enzymes and other proteins as well as in the development of new drugs.
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