|
type |
Journal Article |
authors |
Scapin, G.; Blanchard, J.S. |
title |
Enzymology of bacterial lysine biosynthesis |
journal |
Adv Enzymol Relat Areas Mol Biol |
Activity |
4.1.1.20 |
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 |
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