Homoisocitrate dehydrogenase

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homoisocitrate dehydrogenase
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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
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PMC articles
PubMed articles
NCBI proteins

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

+ NAD+
 
 
 
H+
Homoisocitrate dehydrogenase
 
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.