title: Enzymology of bacterial lysine biosynthesis.
abstract: Bacteria have evolved three strategies for the synthesis of lysine from aspartate via formation of the intermediate diaminopimelate (DAP), a metabolite that is also involved in peptidoglycan formation. The objectives of this chapter are descriptions of mechanistic studies on the reactions catalyzed by dihydrodipicolinate synthase, dihydrodopicolinate reductase, tetrahydrodipicolinate N-succinyl-transferase, N-succinyl-L,L-DAP aminotransferase, N-succinyl-L,L-DAP desuccinylase, L,L-DAP epimerase, L,L-DAP decarboxylase, and DAP dehydrogenase. These enzymes are discussed in terms of kinetic, isotopic, and X-ray crystallographic data that allow one to infer the nature of interactions of each of these enzymes with its substrate(s), coenzymes, and inhibitors.
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
authors.forename: G
authors.initials: G
authors.lastname: Scapin
authors.forename: J S
authors.initials: JS
authors.lastname: Blanchard
mesh_terms: D001222:Aspartate Kinase / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology*; D003960:Diaminopimelic Acid / Q000378:metabolism; D008239:Lysine / Q000096:biosynthesis*; D009161:Mycobacterium / Q000201:enzymology / Q000235:genetics
chemical_list: D003960:Diaminopimelic Acid; D001222:Aspartate Kinase; D008239:Lysine