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Literature summary for 1.1.1.87 extracted from

  • Lin, Y.; Volkman, J.; Nicholas, K.M.; Yamamoto, T.; Eguchi, T.; Nimmo, S.L.; West, A.H.; Cook, P.F.
    Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae (2008), Biochemistry, 47, 4169-4180.
    View publication on PubMed
Search for more literature for 1.1.1.87

Inhibitors

Inhibitors Comment Organism Structure
3-carboxypropylidenemalate
-
 Saccharomyces cerevisiae
Mg-homoisocitrate
-
 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0042
-
 homoisocitrate oxidate decarboxylation of homoisocitrate Saccharomyces cerevisiae
0.09
-
 NADH reductive carboxylation of alpha-ketoadipate Saccharomyces cerevisiae
0.45
-
 NAD+ oxidate decarboxylation of homoisocitrate Saccharomyces cerevisiae
3.2
-
 homoisocitrate reductive carboxylation of alpha-ketoadipate Saccharomyces cerevisiae
16.3
-
 CO2 reductive carboxylation of alpha-ketoadipate Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+ two enzyme groups act as acid-base catalysts in the reaction. A group with a pKa of 6.5-7 acts as a general base accepting a proton as the beta-hydroxy acid is oxidized to the beta-keto acid, and this residue participates in all three of the chemical steps, acting to shuttle a proton between the C2 hydroxyl and itself. The second group acts as a general acid with a pKa of 9.5 and likely catalyzes the tautomerization step by donating a proton to the enol to give the final product Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2(R),3(S)-homoisocitrate + NAD+ with homoisocitrate as the substrate, no primary deuterium isotope effect is observed, and a small 13C kinetic isotope effect indicates that the decarboxylation step contributes only slightly to rate limitation Saccharomyces cerevisiae alpha-ketoadipate + NADH + CO2 + H+
-
 ?
homoisocitrate + NAD+
-
 Saccharomyces cerevisiae alpha-ketoadipate + NADH + CO2 + H+
-
 r
homoisocitrate + NAD+
-
 Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH + H+
-
 r
isocitrate + NAD+
-
 Saccharomyces cerevisiae ?
-
 r
threo-D-isocitric acid + NAD+ with isocitrate as the substrate, primary deuterium and 13C isotope effects indicate that hydride transfer and decarboxylation steps contribute to rate limitation, and that the decarboxylation step is the more rate-limiting of the two. The multiple-substrate deuterium/13C isotope effects suggest a stepwise mechanism with hydride transfer preceding decarboxylation Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
3-carboxy-2-hydroxyadipate dehydrogenase
-
 Saccharomyces cerevisiae
HICDH
-
 Saccharomyces cerevisiae
homoisocitrate dehydrogenase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7
-
 reductive carboxylation Saccharomyces cerevisiae
7.5
-
 oxidative decarboxylation Saccharomyces cerevisiae
25
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
 enzyme is stable when incubated for at least 15 min over the pH range of 5.0-10.0 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.002
-
 Mg-homoisocitrate oxidate decarboxylation of homoisocitrate Saccharomyces cerevisiae