Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
efficacy of association mapping for dissecting natural variation in primary metabolic pathways, the considerable genetic diversity observed in maize CCM genes underlies heritable phenotypic variation in enzyme activities and can be useful to identify putative functional sites
evolution
-
the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues
evolution
-
the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs
evolution
evolutionary relationships of IDHs, overview
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
evolution
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
evolution
-
OtIDH may be an ancestral form of type II IDHs (all other reported members are NADP+-linked enzymes) and may have evolved into NADP+-dependent IDH for adaptation to the increased demand of NADPH under carbon starvation
evolution
phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH). NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs. Type II NAD-IDHs is identified from the marine bacterium Congregibacter litoralis KT71, i.e ClIDH. Evolutionary relationships between 151 IDHs from different organisms, overview
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
-
evolution
-
the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs
-
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
-
evolution
-
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
-
evolution
-
phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH). NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs. Type II NAD-IDHs is identified from the marine bacterium Congregibacter litoralis KT71, i.e ClIDH. Evolutionary relationships between 151 IDHs from different organisms, overview
-
evolution
-
evolutionary relationships of IDHs, overview
-
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
-
malfunction
-
IDH activity is increased in patients with prolonged cell phone daily use over 4 h/day. Its level correlates negatively with either the motility ratio percentages or the progressive motility percentages in the study groups. NAD+-IDH in human seminal plasma can be one of seminal plasma biomarkers reflecting the mitochondrial function of spermatozoa. Alteration of its level reflect the defective motility of sperms among some cases of cellular phone users
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Akt pathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Aktpathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Aktpathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
metabolism
regulatory controls of key enzymes during microbial lipid accumulation involving the enzyme, overview
metabolism
-
yeast IDH is regulated both by allostery and by covalent formation of a disulfide bond, and these regulatory mechanisms contribute to modulation of respiratory metabolism in vivo
metabolism
-
NAD-IDH is a key enzyme in the Krebs cycle
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
-
regulatory controls of key enzymes during microbial lipid accumulation involving the enzyme, overview
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
-
the cofactor swapping of the enzyme from NADPH to NADH decreases the biomass yield of Escherichia coli on acetate
additional information
-
reduction of mitochondrial IDH activity has little effect on the relative electron transport or assimilation rates and a minor reduction in the maximum efficiency of PSII
additional information
-
interactions between sulfhydryl side chains of IDH2 Cys150 residues limit access to eight D-isocitrate and four AMP binding sites. In the presence of dithiothreitol, all ligand binding sites except for two potential NAD+ sites can be occupied
additional information
-
Ser102 plays an important role in substrate binding and is required for the enzyme function
additional information
-
the IDH2 Cys-150 residue controls access to isocitrate binding sites. The wild-type enzyme displays four binding sites for isocitrate and two binding sites for AMP in the absence of dithiothreitol, and these numbers increase to eight and four in the presence of dithiothreitol, respectively
additional information
homology modeling and docking studies of the human NAD-IDHalpha, overview
additional information
-
homology modeling and docking studies of the human NAD-IDHalpha, overview
additional information
-
structure homology modelling, overview. Residue Asp344 is clearly a major determinant of coenzyme specificity in OtIDH and residue Met345 plays critical role in NAD+ recognition and binding