Homoisocitrate dehydrogenase
| homoisocitrate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Homoisocitrate dehydrogenase tetramer, Thermus thermophilus | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.87 | ||||||||
| CAS no. | 37250-23-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction
- (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ 2-oxoadipate + CO2 + NADH + H+
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1X0L.
References
[edit]- Strassman M, Ceci LN (1965). "Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid". J. Biol. Chem. 240 (11): 4357–61. doi:10.1016/S0021-9258(18)97069-9. PMID 4284830.
- Rowley B, Tucci AF (1970). "Homoisocitric dehydrogenase from yeast". Arch. Biochem. Biophys. 141 (2): 499–510. doi:10.1016/0003-9861(70)90167-0. PMID 4395693.
- Zabriskie TM, Jackson MD (2000). "Lysine biosynthesis and metabolism in fungi". Nat. Prod. Rep. 17 (1): 85–97. doi:10.1039/a801345d. PMID 10714900.
