Synthesis and Evaluation of Novel Substrates and Inhibitors of N-Succinyl-ll-diaminopimelate Aminotransferase (DAP-AT) from Escherichia coli
- 1 January 1996
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (32) , 7449-7460
- https://doi.org/10.1021/ja960640v
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Quantum Engineering of Optical NonlinearitiesScience, 1996
- Pyridine and piperidine derivatives as inhibitors of dihydrodipicolinic acid synthase, a key enzyme in the diaminopimelate pathway to l-lysineBioorganic & Medicinal Chemistry Letters, 1994
- Crystal Structures of Escherichia coli Aspartate Aminotransferase in Two Conformations: Comparison of an Unliganded Open and Two Liganded Closed FormsJournal of Molecular Biology, 1994
- Sequential biocatalytic kinetic resolutionsJournal of the American Chemical Society, 1990
- A new synthetic approach to 1-(hydroxymethyl)-8-methoxy-1,2,3,4-tetrahydroisoquinolin-4-oneThe Journal of Organic Chemistry, 1987
- Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structureJournal of Molecular Biology, 1984
- The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactionsTrends in Biochemical Sciences, 1982
- Conversion of acyclic amines to amides by chlorine dioxideThe Journal of Organic Chemistry, 1982
- Oxidations with solid potassium permanganateThe Journal of Organic Chemistry, 1979
- Synthesen in der Phenanthren‐Reihe, V. Mitteil.: Anwendung der Reformatskischen ReaktionBerichte der deutschen chemischen Gesellschaft (A and B Series), 1943