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Literature summary extracted from

  • Miyazaki, J.; Asada, K.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
    Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance (2005), J. Bacteriol., 187, 6779-6788.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.87 purified recombinant enzyme, hanging drop vapour diffusion method, 10 mg/ml protein with reservoir solution containing 24% PEG 400, and 0.1 M citrate, pH 4.8, addition of 0.003 ml drops of 0.1 M MgCl2, 5 mM isocitrate or homoisocitrate, and of a 0.001 ml drop 50 mM CdCl2, equilibration against 0.5 ml reservoir solution, 5 days at 20°C, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.87 V135M site-directed mutagenesis, tetramer-to-dimer structural transition enhances the activity with isocitrate 1.6fold Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.87 0.161
-
 isocitrate pH 7.5, 60°C, recombinant mutant V135M Thermus thermophilus
1.1.1.87 0.521
-
 isocitrate pH 7.5, 60°C, recombinant wild-type enzyme Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.87 Mg2+
-
 Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.87 Thermus thermophilus
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.87 additional information
-
-
 Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.87 homoisocitrate + NAD+
-
 Thermus thermophilus ?
-
 ?
1.1.1.87 isocitrate + NAD+ 20fold preferred to homoisocitrate Thermus thermophilus ?
-
 ?
1.1.1.87 additional information substrate binding site structure, the substrate specificity is determined by residue Arg85, no activity with 3-isopropylmalate Thermus thermophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.87 tetramer subunit interface, crystal structure analysis Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.87 HICDH
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.87 60
-
 assay at Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.87 211
-
 isocitrate pH 7.5, 60°C, recombinant mutant V135M Thermus thermophilus
1.1.1.87 438
-
 isocitrate pH 7.5, 60°C, recombinant wild-type enzyme Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.87 7.5
-
 assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.87 NAD+
-
 Thermus thermophilus