Alternate substrates and inhibitors of 1-aminocyclopropane-1-carboxylic acid synthase
Autor: | Shahrokh Khani-Oskouee, Douglas M. Kalvin, Ronald W. Woodard, Kondareddiar Ramalingam |
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Rok vydání: | 1987 |
Předmět: |
chemistry.chemical_classification
Purine Methionine biology ATP synthase Chemistry Stereochemistry Organic Chemistry food and beverages Substrate (chemistry) Active site Biochemistry Adenosine chemistry.chemical_compound Enzyme Drug Discovery biology.protein medicine 1-Aminocyclopropane-1-carboxylic acid Molecular Biology medicine.drug |
Zdroj: | Bioorganic Chemistry. 15:92-99 |
ISSN: | 0045-2068 |
Popis: | Structural analogs of (−)- S -adenosyl- l -methionine (SAM), in which the heterocyclic base was modified, were used to initiate studies to elucidate the active site conformation of the enzyme 1-aminocyclopropane-1-carboxylic acid (ACC) synthase, which was partially purified from Lycopersicon esculentum (tomato). These potential substrate analogs were screened for activity both as substrates and/or as inhibitors of ACC synthase. In general, ACC synthase was found to have a rather rigid specificity for the structural features of the natural substrate (SAM) in that only the purine base adenosine and adenosine analogs in which the N 6 nitrogen was modified were substrates. |
Databáze: | OpenAIRE |
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