Homoisocitrate dehydrogenase

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

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
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PMCarticles
PubMedarticles
NCBIproteins
(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

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

References

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  • 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.