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Literature summary for 1.1.1.42 extracted from

  • Quartararo, C.E.; Hazra, S.; Hadi, T.; Blanchard, J.S.
    Structural, kinetic and chemical mechanism of isocitrate dehydrogenase-1 from Mycobacterium tuberculosis (2013), Biochemistry, 52, 1765-1775.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene Rv3339c, expression of N-terminally His6-tagged enzyme Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified ICDH-1 in complex with NADPH at Mn2+, hanging drop vapor diffusion method, 0.001 ml of protein in 5 mM NADPH, and 5 mM MnCl2 is mixed with 0.001 ml of reservoir solution containing 30% PEG 2000 and 0.1 M Tris-HCl, pH 8.0, room temperature, X-ray diffraction structure determination and analysis at 2.18 A resoltuion Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate noncompetitive versus NADP+ Mycobacterium tuberculosis
malate noncompetitive versus NADP+ and isocitrate Mycobacterium tuberculosis
additional information product inhibition patterns for ICDH-1, overview Mycobacterium tuberculosis
NADPH product inhibition competitive versus NADP+ and noncompetitive versus isocitrate Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics, kinetic mechanism of ICDH-1, overview Mycobacterium tuberculosis
0.015
-
NADP+ pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme Mycobacterium tuberculosis
0.05
-
isocitrate pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate + NADP+ Mycobacterium tuberculosis
-
2-oxoglutarate + CO2 + NADPH + H+
-
?
isocitrate + NADP+ Mycobacterium tuberculosis H37Rv
-
2-oxoglutarate + CO2 + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WKL1 gene Rv3339c
-
Mycobacterium tuberculosis H37Rv P9WKL1 gene Rv3339c
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged enzyme by nickel affinity chromatography and gel filtration Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ protonation of the enolate to form product 2-oxoglutarate is the rate-limiting step Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate + NADP+
-
Mycobacterium tuberculosis 2-oxoglutarate + CO2 + NADPH + H+
-
?
isocitrate + NADP+
-
Mycobacterium tuberculosis H37Rv 2-oxoglutarate + CO2 + NADPH + H+
-
?
additional information Mycobacterium tuberculosis ICDH-1 also catalyzes the formation of 2-hydroxyglutarate Mycobacterium tuberculosis ?
-
?
additional information Mycobacterium tuberculosis ICDH-1 also catalyzes the formation of 2-hydroxyglutarate Mycobacterium tuberculosis H37Rv ?
-
?

Subunits

Subunits Comment Organism
homodimer each subunit has a Rossmann fold, and a common top domain of interlocking beta sheets Mycobacterium tuberculosis
More three-dimensional structure of Mtb ICDH-1, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ICDH
-
Mycobacterium tuberculosis
ICDH-1
-
Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
33
-
NADP+ pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme Mycobacterium tuberculosis
33
-
isocitrate pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Mycobacterium tuberculosis