1.1.1.87: homoisocitrate dehydrogenase

This is an abbreviated version, for detailed information about homoisocitrate dehydrogenase, go to the full flat file.

Reaction

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
+
NAD+
=
2-oxoadipate
+
CO2
+
NADH
+
H+

Synonyms

(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating), 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), dehydrogenase, homoisocitrate, EC 1.1.1.155, HIc, HIc dehydrogenase, HICDH, homoisocitrate dehydrogenase, homoisocitric dehydrogenase, isocitrate-homoisocitrate dehydrogenase, protein PH1722, ScHICDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.87 homoisocitrate dehydrogenase

General Information

General Information on EC 1.1.1.87 - homoisocitrate dehydrogenase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the family of pyridine dinucleotide-dependent beta-hydroxyacid oxidative decarboxylating dehydrogenases, specifically the family that has (R)-beta-hydroxyacid substrates, including isocitrate dehydrogenase (ICDH) among others. Superposition of available structures of the malic enzyme, isopropylmalate dehydrogenase, IcDH, and HIcDH show a similar overall geometry of residues in the substrate and metal ion binding sites. A Lys (general base)-Tyr (general acid) pair is conserved among these enzymes. The similar structural geometry in the active site suggests a similar general chemical mechanism. Three aspartate residues are conserved in the active sites of all HIcDHs sequenced to data, and are also conserved across the family of pyridine nucleotide-dependent oxidative decarboxylases including malic enzyme
metabolism
additional information