EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O |
involved in L-lysine biosynthesis |
Corynebacterium glutamicum ATCC 13032 |
(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+ |
it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme |
Corynebacterium glutamicum |
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O |
- |
? |
1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ |
it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme |
Corynebacterium glutamicum ATCC 13032 |
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O |
- |
? |
1.17.1.8 | 2,3-dihydrodipicolinate + NAD(P)H |
lysine and diaminopimelate biosynthesis pathway |
Escherichia coli |
2,3,4,5-tetrahydrodipicolinate + NAD(P)+ |
- |
? |
1.17.1.8 | 2,3-dihydrodipicolinate + NAD(P)H |
no regulatory effect of lysine |
Brevibacillus brevis |
2,3,4,5-tetrahydrodipicolinate + NAD(P)+ |
- |
? |
1.17.1.8 | 2,3-dihydrodipicolinate + NAD(P)H |
repressed by lysine |
Lysinibacillus sphaericus |
2,3,4,5-tetrahydrodipicolinate + NAD(P)+ |
- |
? |
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 |
Mycobacterium tuberculosis |
2,3,4,5-tetrahydrodipicolinate + NAD(P)+ |
- |
? |
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 |
Mycobacterium tuberculosis H37Rv |
2,3,4,5-tetrahydrodipicolinate + NAD(P)+ |
- |
? |
1.17.1.8 | pyridine dicarboxylate + NADH + H+ |
stable substrate analog, 25 mM phosphate D2O (deuterium water) buffer, pH 7.8 for NMR analysis of binding interactions with saturation transfer difference titration studies at 298 K (25°C) |
Escherichia coli |
reduced pyridine dicarboxylate + NAD+ |
- |
? |
1.17.1.8 | dihydrodipicolinate + NADH + H+ |
substrate dihydrodipicolinate is instable |
Escherichia coli |
tetrahydrodipicolinate + NAD+ |
- |
? |