Homoisocitrate dehydrogenase

homoisocitrate dehydrogenase
Homoisocitrate dehydrogenase tetramer, Thermus thermophilus
Identifiers
EC no.1.1.1.87
CAS no.37250-23-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
+ CO2 + NADH
 

The two substrates of this enzyme are (-)-homoisocitric acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 2-oxoadipic acid, carbon dioxide, reduced NADH, and a proton.[1][2][3][4]

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

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1X0L.

References

  1. ^ Enzyme 1.1.1.87 at KEGG Pathway Database.
  2. ^ 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.
  3. ^ 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.
  4. ^ Zabriskie TM, Jackson MD (2000). "Lysine biosynthesis and metabolism in fungi". Nat. Prod. Rep. 17 (1): 85–97. doi:10.1039/a801345d. PMID 10714900.