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B6db references: 9559056

type Journal Article
authors Scapin, G.; Blanchard, J.S.
title Enzymology of bacterial lysine biosynthesis
journal Adv Enzymol Relat Areas Mol Biol
sel selected
ui 9559056
year (1998)
volume 72
pages 279-324
keywords Amino Acids, Lysine
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.
last changed 2008/01/22 12:57

B6db references