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Literature summary extracted from

  • Gabriel, I.; Vetter, N.D.; Palmer, D.R.; Milewska, M.J.; Wojciechowski, M.; Milewski, S.
    Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug (2013), FEMS Yeast Res., 13, 143-155.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.87 expression of His-tagged enzyme in Escherichia coli strain TOP 10F' Candida albicans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.87 (2R,3S)-3-(p-carboxybenzyl)malate
-
 Candida albicans
1.1.1.87 (2S)-thiahomocitrate
-
 Candida albicans
1.1.1.87 additional information inhibitor docking study, molecular modeling of CaHIcDH-inhibitor interaction, overview Candida albicans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.87 0.042
-
 NAD+ native enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.074
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.45
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate native enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 1.09
-
 NAD+ recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.87 K+ dependent on Candida albicans
1.1.1.87 Mg2+ dependent on Candida albicans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.87 41491
-
 4 * 42600, SDS-PAGE, x * 41491, sequence calculation Candida albicans
1.1.1.87 42600
-
 4 * 42600, SDS-PAGE, x * 41491, sequence calculation Candida albicans
1.1.1.87 158000
-
 gel filtration Candida albicans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Candida albicans strict specificity for homoisocitrate 2-oxoadipate + CO2 + NADH + H+
-
 ?
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Candida albicans ATCC 10231 strict specificity for homoisocitrate 2-oxoadipate + CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.87 Candida albicans
-
 gene LYS12
-
1.1.1.87 Candida albicans ATCC 10231
-
 gene LYS12
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.87 recombinant His-tagged enzyme from Escherichia coli strain TOP 10F by nickel affinity chromatography' Candida albicans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate Candida albicans 2-oxoadipate + CO2 + NADH + H+
-
 ?
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex Candida albicans 2-oxoadipate + CO2 + NADH + H+
-
 ?
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate Candida albicans ATCC 10231 2-oxoadipate + CO2 + NADH + H+
-
 ?
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex Candida albicans ATCC 10231 2-oxoadipate + CO2 + NADH + H+
-
 ?
1.1.1.87 additional information substrate docking study Candida albicans ?
-
 ?
1.1.1.87 additional information substrate docking study Candida albicans ATCC 10231 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.87 More three-dimensional structure and homology modeling, overview Candida albicans
1.1.1.87 tetramer 4 * 42600, SDS-PAGE, x * 41491, sequence calculation Candida albicans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.87 HICDH
-
 Candida albicans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.87 20
-
 assay at Candida albicans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.87 0.38
-
 NAD+ recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.38
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.4
-
 NAD+ native enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.4
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate native enzyme, pH 7.8, 20°C Candida albicans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.87 7.8
-
 assay at Candida albicans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.87 NAD+
-
 Candida albicans

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.87 0.000097
-
 recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans (2S)-thiahomocitrate
1.1.1.87 2.97
-
 recombinant His-tagged enzyme, pH 7.8, 20°C, competitive versus (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate Candida albicans (2R,3S)-3-(p-carboxybenzyl)malate
1.1.1.87 3.78
-
 recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans (2R,3S)-3-(p-carboxybenzyl)malate

General Information

EC Number General Information Comment Organism
1.1.1.87 additional information three-dimensional structure and homology modeling, overview Candida albicans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.87 0.35
-
 NAD+ recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 0.44
-
 NAD+ native enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 5.16
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans
1.1.1.87 8.75
-
 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate native enzyme, pH 7.8, 20°C Candida albicans