Abstract
Dipeptide substrates of N-Succinyl Diaminopimelic Acid Aminotransferase (DAP-AT) were converted to hydrazines by treatment with hydrazine and cyanoborohydride. These compounds were tested in vitro as inhibitors of DAP-AT from E. coli and in vivo as antibiotics. The hydrazino-dipeptides showed potent slow binding slow binding inhibition of DAP-AT as well as antimicrobial activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / chemical synthesis*
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology
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Dipeptides / chemical synthesis*
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Dipeptides / chemistry
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Dipeptides / pharmacology
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology
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Escherichia coli / enzymology*
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Glutamate Dehydrogenase / antagonists & inhibitors
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Hydrazines / chemical synthesis*
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Hydrazines / chemistry
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Hydrazines / pharmacology
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Indicators and Reagents
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Kinetics
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Molecular Structure
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Structure-Activity Relationship
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Substrate Specificity
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Succinyldiaminopimelate Transaminase
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Transaminases / antagonists & inhibitors*
Substances
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Anti-Bacterial Agents
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Dipeptides
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Enzyme Inhibitors
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Hydrazines
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Indicators and Reagents
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Glutamate Dehydrogenase
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Transaminases
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Succinyldiaminopimelate Transaminase