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Literature summary for extracted from

  • Nango, E.; Yamamoto, T.; Kumasaka, T.; Eguchi, T.
    Structure of Thermus thermophilus homoisocitrate dehydrogenase in complex with a designed inhibitor (2011), J. Biochem., 150, 607-614.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in binary complex with inhibitor (2S,3S)-thiahomoisocitrate, sitting drop vapour diffusion method, 0.00 ml of 8.7 mg/ml protein in 5 mM Tris-HCl, pH 7.8. 0.8 mM inhibitor, and 1.7 mM NAD, is mixed with 0.002 ml of reservoir solution containing 40% 2-methyl-2,4-pentandiol and 100 mM citrate pH 4.85, eqilibration against 1 ml resetvoir solution, X-ray diffrcation structure determination and analysis at 2.6 A resolution, molecular replacement Thermus thermophilus


Inhibitors Comment Organism Structure
(2S,3S)-(-)-3-methylmercaptomalic acid
Thermus thermophilus
(2S,3S)-thiahomoisocitrate interacts through hydrogen bonding to Arg 118, Tyr 125 and Lys 171 in the active site, enzyme binding structure, overview Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate pH 7.8, 60°C Thermus thermophilus


Metals/Ions Comment Organism Structure
Mg2+ essentially required Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Thermus thermophilus
2-oxoadipate + CO2 + NADH + H+


Organism UniProt Comment Textmining
Thermus thermophilus Q5SIJ1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
Thermus thermophilus 2-oxoadipate + CO2 + NADH + H+
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ i.e. (2R,3S)-homoisocitrate Thermus thermophilus 2-oxoadipate + CO2 + NADH + H+


Synonyms Comment Organism
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
assay at Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
assay at Thermus thermophilus


Cofactor Comment Organism Structure
Thermus thermophilus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
(2S,3S)-thiahomoisocitrate pH 7.8, 60°C Thermus thermophilus

General Information

General Information Comment Organism
metabolism homoisocitrate dehydrogenase is involved in the alpha-aminoadipate pathway of lysine biosynthesis Thermus thermophilus