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Literature summary extracted from
- Structural insight into dihydrodipicolinate reductase from Corynebacterium glutamicum for lysine biosynthesis (2016), J. Microbiol. Biotechnol., 26, 226-232 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.17.1.8 | expression in an Escherichia coli B834 strain | Corynebacterium glutamicum |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.17.1.8 | crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, determined at 2.5 A resolution. The crystal belongs to the I4(1)22 space group, and the asymmetric unit of the crystal contains two CgDapB molecules | Corynebacterium glutamicum |
| 1.17.1.8 | crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, hanging-drop vapor-diffusion method at 20°C, crystal structure of the enzyme is determined at 2.5 A resolution | Corynebacterium glutamicum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ | Corynebacterium glutamicum | the enzyme is involved in L-lysine biosynthesis | (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+ | Corynebacterium glutamicum ATCC 13032 | the enzyme is involved in L-lysine biosynthesis | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O | - |
? | |
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O | Corynebacterium glutamicum | involved in L-lysine biosynthesis | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ | - |
? | |
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O | Corynebacterium glutamicum ATCC 13032 | involved in L-lysine biosynthesis | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.1.8 | Corynebacterium glutamicum | P40110 | - |
- |
| 1.17.1.8 | Corynebacterium glutamicum ATCC 13032 | P40110 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.17.1.8 | - |
Corynebacterium glutamicum |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ | the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 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 | 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 | (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+ | the enzyme is involved in L-lysine biosynthesis | Corynebacterium glutamicum ATCC 13032 | (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 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O | involved in L-lysine biosynthesis | Corynebacterium glutamicum | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ | - |
? | |
| 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 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+ | - |
? | |
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum ATCC 13032 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+ | - |
? | |
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+ | - |
? | |
| 1.17.1.8 | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum ATCC 13032 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.1.8 | tetramer | 4 * 260240, calculated from sequence | Corynebacterium glutamicum |
| 1.17.1.8 | tetramer | each protomer is composed of two domains, an N-terminal domain and a C-terminal domain. The N-terminal domain mainly contributes to nucleotide binding, whereas the C-terminal domain is involved in substrate binding | Corynebacterium glutamicum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.1.8 | DapB | - |
Corynebacterium glutamicum |
| 1.17.1.8 | dihydrodipicolinate reductase | - |
Corynebacterium glutamicum |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.1.8 | NADH | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum | |
| 1.17.1.8 | NADH | the enzyme utilizes both NADH and NADPH as cofactors. The mode of cofactor binding to the enzyme is elucidated by determining the crystal structure of the enzyme in complex with NADP+ | Corynebacterium glutamicum | |
| 1.17.1.8 | NADPH | the enzyme utilizes both NADH and NADPH as cofactors | Corynebacterium glutamicum | |
| 1.17.1.8 | NADPH | the enzyme utilizes both NADH and NADPH as cofactors. The mode of cofactor binding to the enzyme is elucidated by determining the crystal structure of the enzyme in complex with NADP+ | Corynebacterium glutamicum | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.17.1.8 | metabolism | the enzyme is involved in L-lysine biosynthesis | Corynebacterium glutamicum |
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