1.17.1.8	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+	-	
1.17.1.8	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+	the enzyme catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants	
1.17.1.8	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+	the enzyme catalyzes the second committed step in the diaminopimelate/lysine anabolic pathways	
1.17.1.8	(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+	the enzyme is involved in L-lysine biosynthesis	
1.17.1.8	(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O	involved in L-lysine biosynthesis	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	-	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	highest activity during exponential growth phase	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	no regulatory effect of lysine	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	lysine and diaminopimelate biosynthesis pathway	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	determination of metabolic block in the pathway in mutant M-203	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	essentially involved in cell wall synthesis	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	repressed by lysine	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	second step in the biosynthesis of meso-diaminopimelate, a bacterial cell wall component, and is involved in L-lysine biosynthesis	
1.17.1.8	2,3-dihydrodipicolinate + NAD(P)H	enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants	
1.17.1.8	dihydrodipicolinate + NADH + H+	substrate dihydrodipicolinate is instable	
1.17.1.8	additional information	DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate