Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.87 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
Search for more literature for 1.1.1.87

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

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+ Candida albicans strict specificity for homoisocitrate 2-oxoadipate + CO2 + NADH + H+
-
 ?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Candida albicans ATCC 10231 strict specificity for homoisocitrate 2-oxoadipate + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Candida albicans
-
 gene LYS12
-
Candida albicans ATCC 10231
-
 gene LYS12
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate Candida albicans 2-oxoadipate + CO2 + NADH + H+
-
 ?
(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+
-
 ?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate Candida albicans ATCC 10231 2-oxoadipate + CO2 + NADH + H+
-
 ?
(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+
-
 ?
additional information substrate docking study Candida albicans ?
-
 ?
additional information substrate docking study Candida albicans ATCC 10231 ?
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
HICDH
-
 Candida albicans

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Candida albicans

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000097
-
 recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans (2S)-thiahomocitrate
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
3.78
-
 recombinant His-tagged enzyme, pH 7.8, 20°C Candida albicans (2R,3S)-3-(p-carboxybenzyl)malate

General Information

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

kcat/KM [mM/s]

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