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Literature summary for 1.1.1.41 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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli
NADP+
-
Escherichia coli