Bestatin-derived analogs inhibit E. coli methionine aminopeptidase
- 1 January 1994
- book chapter
- Published by Springer Nature
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzymeBiochemistry, 1993
- Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis.Proceedings of the National Academy of Sciences, 1991
- Hydrolysis of dansyl-peptide substrates by leucine aminopeptidase: origin of dansyl fluorescence changes during hydrolysisBiochemistry, 1988
- Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structureJournal of Bacteriology, 1987
- Synthesis of (2S,3R)-3-amino-2-hydroxy-5-methylhexanoic acid derivatives. Application to the synthesis of amastatin, an inhibitor of aminopeptidasesThe Journal of Organic Chemistry, 1980
- Synthesis and structure-activity relations of bestatin analogs, inhibitors of aminopeptidase BJournal of Medicinal Chemistry, 1977