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Literature summary extracted from

  • Hurley, J.H.; Chen, R.; Dean, A.M.
    Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ to NAD+ specificity-reversal mutant (1996), Biochemistry, 35, 5670-5678.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.41 crystallization in artificial mother liquor supplemented with 100 mM NAD+ Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.41 C201M/C332Y/K344D/Y345I/V351A/Y391K/R395S converts the cofactor specificity from 7000-fold preference of NADP+ to a 200-fold preference of NAD+ Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.41 0.017
-
 NADP+ wild type Escherichia coli
1.1.1.41 0.099
-
 NAD+ 7-fold mutant Escherichia coli
1.1.1.41 4.7
-
 NAD+ wild type Escherichia coli
1.1.1.41 5.8
-
 NADP+ 7-fold mutant Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.41 isocitrate + NAD+ Escherichia coli
-
 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.41 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.41 isocitrate + NAD+
-
 Escherichia coli 2-oxoglutarate + CO2 + NADH + H+
-
 ?
1.1.1.41 isocitrate + NADP+
-
 Escherichia coli 2-oxoglutarate + CO2 + NADPH + H+
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.41 NAD+
-
 Escherichia coli
1.1.1.41 NADP+
-
 Escherichia coli