Anticapsin, an active-site directed irreversible inhibitor of glucosamine-6-phosphate synthetase from Escherichia coli
| Autor: | Edward Borowski, Hans Zähner, Henryk Chmara |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Glutamine
Glucose-6-Phosphate medicine.disease_cause Drug Discovery Escherichia coli medicine Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) Pharmacology Alanine Glucosamine Binding Sites biology Glucosephosphates Active site biology.organism_classification Enterobacteriaceae Kinetics Mechanism of action Biochemistry Enzyme inhibitor biology.protein medicine.symptom Carbohydrate Epimerases Bacteria |
| Zdroj: | The Journal of Antibiotics. 37:1038-1043 |
| ISSN: | 1881-1469 0021-8820 |
| DOI: | 10.7164/antibiotics.37.1038 |
| Popis: | Glucosamine-6-phosphate synthetase from Escherichia coli K-12 is progressively inactivated L-beta-(2,3-epoxycyclohexyl-4-on)alanine (anticapsin). With increasing concentrations of anticapsin the reaction exhibits rate saturation: the minimum inactivation half-time is 1.15 minutes, with a Kin alpha ct of 2.5 microM. Glutamine and competitive inhibitors protect against inactivation. Fructose-6-phosphate promotes the inactivation rate. It is concluded that anticapsin is an active-site directed glutamine analog in the reaction catalyzed by glucosamine-6-phosphate synthetase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|