Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO 2.

Feb 28, 2025 · We present CatPred, a deep learning framework for predicting in vitro enzyme kinetic parameters, including turnover numbers (kcat), Michaelis constants (Km), and inhibition constants (Ki).

ABSTRACT: Two site-directed mutants of isocitrate dehydrogenase (IDH) of Escherichia coli have been studied by site-directed mutagenesis kinetic and structural studies. Substitution of phenylalanine for tyrosine at position 160 (Y160F) showed 0.4% of the kcat of wild-type with isocitrate as substrate, while the Km for isocitrate remained unchanged.

Isocitrate dehydrogenase 1 (IDH1) catalyzes the reversible NADP+-dependent conversion of isocitrate to α-ketoglutarate (αKG) to provide critical cytosolic substrates and drive NADPH-dependent...

The kcat/Km values of PaIDH2 for NADP + and ICT were 4.42 μM −1 s −1 and 7.26 μM −1 s −1, respectively. PaIDH2, MtIDH2 and AbIDH2 were classified as type III-IDH enzymes.

We determined the Michaelis constant (K (m)) and maximal velocity (Vmax) of lactate dehydrogenase (LDH) in periportal hepatocytes and skeletal muscle fibers by three different histochemical assay methods.

Mar 13, 2025 · We applied KcatNet to genome-scale Kcat prediction across diverse yeast species, improving proteome allocation predictions by integrating its outputs into metabolic models. Experimental validation further confirmed the model's ability to identify enzyme mutants with enhanced activity.

the mutant exhibits an about 170fold decrease in catalytic efficiency, driven by a 5.4fold decrease in kcat and 31fold increase in Km as compared to the wild type enzyme.

The catalytic efficiencies (kcat/Km) of ScIDH1 R148H and YlIDH R141H for isocitrate oxidation were drastically reduced by 227-fold and 460-fold, respectively, of those of the wild-type enzymes.

Aug 9, 1996 · Isocitrate dehydrogenase (IDH) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase. In addition to the kinase and phosphatase activities, this protein catalyzes an intrinsic ATPase reaction.