| 4-hydroxy-tetrahydrodipicolinate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Dihydrodipicolinate reductase tetramer, Corynebacterium glutamicum | |||||||||
| Identifiers | |||||||||
| EC no. | 1.17.1.8 | ||||||||
| CAS no. | 9055-46-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) is an enzyme that catalyzes the chemical reaction
- (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
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + HThe 3 substrates of this enzyme are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, NAD or NADP, and H2O, whereas its 3 products are (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, NADH or NADPH, and H.
This enzyme participates in lysine biosynthesis.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD or NADP as acceptor. The systematic name of this enzyme class is (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+ 4-oxidoreductase. Other names in common use include:
- dihydrodipicolinate reductase,
- dihydrodipicolinic acid reductase, and
- 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase.
References
Further reading
- Farkas W, Gilvarg C (Dec 1965). "The reduction step in diaminopimelic acid biosynthesis". The Journal of Biological Chemistry. 240 (12): 4717–22. doi:10.1016/S0021-9258(18)97014-6. PMID 4378965.
- Tamir H (1971). "Dihydrodipicolinic acid reductase (Escherichia coli)". Metabolism of Amino Acids and Amines Part B. Methods Enzymol. Vol. 17B. pp. 134–139. doi:10.1016/0076-6879(71)17030-9. ISBN 978-0-12-181877-7.
- Devenish SR, Blunt JW, Gerrard JA (Jun 2010). "NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase". Journal of Medicinal Chemistry. 53 (12): 4808–12. doi:10.1021/jm100349s. PMID 20503968.
| Other oxidoreductases (EC 1.15–1.21) | |
|---|---|
| 1.15: Acting on superoxide as acceptor | |
| 1.16: Oxidizing metal ions | |
| 1.17: Acting on CH or CH2 groups | |
| 1.18: Acting on iron–sulfur proteins as donors | |
| 1.19: Acting on reduced flavodoxin as donor | |
| 1.20: Acting on phosphorus or arsenic in donors | |
| 1.21: Acting on X-H and Y-H to form an X-Y bond | |
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