EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.41 | gene HMPREF1139_0890, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli | Campylobacter sp. |
1.1.1.41 | gene icd, sequence comparisons and phylogenetic analysis | Campylobacter curvus |
1.1.1.41 | gene icd, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | gene IDHP, sequence comparisons and phylogenetic analysis | Micromonas commoda |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.41 | D326R/M327H | site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH Asp326/Met327 is completely reversed from NAD+ to NADP+ | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | D326X/M327X | site-directed mutagenesis, the coenzyme specificity of the mutant OlIDH R326H327 is completely reversed from NAD+ to NADP+ | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | L584H/D595R | site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH H584/R595 is completely reversed from NAD+ to NADP+ | Campylobacter sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.41 | Ca2+ | complete inhibition at 2 mM | Campylobacter sp. | |
1.1.1.41 | Cu2+ | complete inhibition at 2 mM | Campylobacter sp. | |
1.1.1.41 | Cu2+ | complete inhibition at 2 mM | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | Zn2+ | complete inhibition at 2 mM | Campylobacter sp. | |
1.1.1.41 | Zn2+ | complete inhibition at 2 mM | Ostreococcus sp. 'lucimarinus' |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.41 | 0.0082 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 0.0114 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 0.0289 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 0.0742 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 0.126 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 0.136 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 0.476 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 0.493 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 0.513 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 1.827 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 2.211 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 2.948 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.41 | Ca2+ | activates, 13.6% activity compared to Mg2+ for OlIDH | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | Co2+ | activates, 35.5% activity compared to Mg2+ for CaIDH | Campylobacter sp. | |
1.1.1.41 | Mg2+ | activates, 68.6% activity compared to Mg2+ for OlIDH | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | Mg2+ | activates, 78.3% activity compared to Mg2+ for CaIDH | Campylobacter sp. | |
1.1.1.41 | Mn2+ | activates, Mn2+ is the most favorable cation for CaIDH | Campylobacter sp. | |
1.1.1.41 | Mn2+ | activates, Mn2+ is the most favorable cation for OlIDH | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | additional information | divalent cations are required for activity | Micromonas commoda | |
1.1.1.41 | additional information | divalent cations are required for activity | Campylobacter curvus | |
1.1.1.41 | additional information | divalent cations are required for activity, low or poor activation by Co2+, Ni2+, K+, Na+, and Li+ | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | additional information | divalent cations are required for activity, low or poor activation by Rb+, Ni2+, K+, Na+, and Li+ | Campylobacter sp. | |
1.1.1.41 | Rb+ | activates, 11.0% activity compared to Mg2+ for OlIDH | Ostreococcus sp. 'lucimarinus' |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.41 | 45000 | - |
- |
Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | 80000 | - |
- |
Campylobacter sp. |
1.1.1.41 | 81000 | - |
recombinant His6-tagged enzyme, gel filtration | Campylobacter sp. |
1.1.1.41 | 92000 | - |
recombinant His6-tagged enzyme, gel filtration | Ostreococcus sp. 'lucimarinus' |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.41 | isocitrate + NAD+ | Ostreococcus sp. 'lucimarinus' | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Micromonas commoda | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Campylobacter sp. | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Campylobacter curvus | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Campylobacter curvus 525.92 | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Campylobacter sp. FOBRC14 | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Micromonas commoda RCC299 | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | Ostreococcus sp. 'lucimarinus' CCE9901 | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.41 | Campylobacter curvus | A0A0M4S9Q1 | - |
- |
1.1.1.41 | Campylobacter curvus 525.92 | A0A0M4S9Q1 | - |
- |
1.1.1.41 | Campylobacter sp. | J4X756 | - |
- |
1.1.1.41 | Campylobacter sp. FOBRC14 | J4X756 | - |
- |
1.1.1.41 | Micromonas commoda | C1E5X2 | - |
- |
1.1.1.41 | Micromonas commoda RCC299 | C1E5X2 | - |
- |
1.1.1.41 | Ostreococcus sp. 'lucimarinus' | - |
- |
- |
1.1.1.41 | Ostreococcus sp. 'lucimarinus' | A4SBK5 | - |
- |
1.1.1.41 | Ostreococcus sp. 'lucimarinus' CCE9901 | - |
- |
- |
1.1.1.41 | Ostreococcus sp. 'lucimarinus' CCE9901 | A4SBK5 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.41 | recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli | Campylobacter sp. |
1.1.1.41 | recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli | Ostreococcus sp. 'lucimarinus' |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.41 | 3.8 | - |
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+ | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | 8.7 | - |
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+ | Campylobacter sp. |
1.1.1.41 | 53.2 | - |
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+ | Campylobacter sp. |
1.1.1.41 | 72.3 | - |
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+ | Ostreococcus sp. 'lucimarinus' |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.41 | isocitrate + NAD+ | - |
Ostreococcus sp. 'lucimarinus' | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Micromonas commoda | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Campylobacter sp. | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Campylobacter curvus | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Campylobacter curvus 525.92 | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Campylobacter sp. FOBRC14 | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Micromonas commoda RCC299 | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NAD+ | - |
Ostreococcus sp. 'lucimarinus' CCE9901 | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Micromonas commoda | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Campylobacter sp. | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Campylobacter curvus | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Ostreococcus sp. 'lucimarinus' | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Campylobacter curvus 525.92 | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Campylobacter sp. FOBRC14 | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Micromonas commoda RCC299 | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.41 | isocitrate + NADP+ | very low activity | Ostreococcus sp. 'lucimarinus' CCE9901 | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.41 | homodimer | - |
Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | homodimer | - |
Micromonas commoda |
1.1.1.41 | homodimer | 2 * 45000, recombinant His6-tagged enzyme, SDS-PAGE | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | monomer | - |
Campylobacter curvus |
1.1.1.41 | monomer | 1 * 80000, recombinant His6-tagged enzyme, SDS-PAGE | Campylobacter sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.41 | CaIDH | - |
Campylobacter sp. |
1.1.1.41 | CcIDH | - |
Campylobacter curvus |
1.1.1.41 | MiIDH | - |
Micromonas commoda |
1.1.1.41 | monomeric NAD-IDH | - |
Campylobacter sp. |
1.1.1.41 | monomeric NAD-IDH | - |
Campylobacter curvus |
1.1.1.41 | OlIDH | - |
Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | type II homodimeric NAD-IDH | - |
Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | type II homodimeric NAD-IDH | - |
Micromonas commoda |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.41 | 25 | - |
assay at | Micromonas commoda |
1.1.1.41 | 25 | - |
assay at | Campylobacter curvus |
1.1.1.41 | 40 | - |
with Mn2+ | Campylobacter sp. |
1.1.1.41 | 40 | - |
with Mg2+ or Mn2+ | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | 45 | - |
with Mg2+ | Campylobacter sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.41 | 40 | 55 | recombinant CaIDH retains the majority of the activity below 45°C, its activity drops rapidly as the temperature is raised. Incubation at 55°C for 20 min causes a 55% or 75% loss of activity in the presence of Mg2+ or Mn2+, respectively | Campylobacter sp. |
1.1.1.41 | 45 | 50 | recombinant OlIDH is stable below 45°C, but its activity rapidly declines as the temperature is raised. Incubation at 45°C for 20 min causes a 28% or 21% loss of activity in the presence of Mg2+ or Mn2+, respectively, whereas incubation at 50°C causes a 91% or 84% loss of activity in the presence of Mg2+ or Mn2+, respectively | Ostreococcus sp. 'lucimarinus' |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.41 | 1.4 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 1.8 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 1.9 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 2 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 4.2 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 7 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 9.5 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 10 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 10.8 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 22.5 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 29.1 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 60.6 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.41 | 7.5 | - |
assay at | Micromonas commoda |
1.1.1.41 | 7.5 | - |
assay at | Campylobacter curvus |
1.1.1.41 | 7.5 | - |
with Mn2+ | Campylobacter sp. |
1.1.1.41 | 8 | - |
with Mg2+ | Campylobacter sp. |
1.1.1.41 | 8.5 | - |
with Mn2+ | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | 9 | - |
with Mg2+ | Ostreococcus sp. 'lucimarinus' |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.41 | NAD+ | specific for, the enzyme displays 224fold preference for NAD+ over NADP+ | Micromonas commoda | |
1.1.1.41 | NAD+ | specific for, the enzyme displays 37fold preference for NAD+ over NADP+ | Campylobacter curvus | |
1.1.1.41 | NAD+ | specific for, the enzyme displays 61fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Leu584 and Asp595 in CaIDH | Campylobacter sp. | |
1.1.1.41 | NAD+ | specific for, the enzyme displays 99fold preference for NAD+ over NADP+ | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | NAD+ | specific for, the enzyme displays 99fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Asp326 and Met327 in OlIDH | Ostreococcus sp. 'lucimarinus' |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.41 | evolution | evolutionary relationships of IDHs, overview | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | 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 | Ostreococcus sp. 'lucimarinus' |
1.1.1.41 | evolution | evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes | Campylobacter sp. |
1.1.1.41 | evolution | evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes | Campylobacter curvus |
1.1.1.41 | evolution | evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes | Micromonas commoda |
1.1.1.41 | 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 | Micromonas commoda |
1.1.1.41 | 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 | Campylobacter sp. |
1.1.1.41 | 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 | Campylobacter curvus |
1.1.1.41 | 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 | Ostreococcus sp. 'lucimarinus' |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.41 | 0.8 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 4 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 4 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 4.5 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 10 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 19.3 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 146 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter curvus | |
1.1.1.41 | 179 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Micromonas commoda | |
1.1.1.41 | 220 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H | Ostreococcus sp. 'lucimarinus' | |
1.1.1.41 | 242 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Campylobacter sp. | |
1.1.1.41 | 368 | - |
NADP+ | pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R | Campylobacter sp. | |
1.1.1.41 | 444 | - |
NAD+ | pH 75, 25°C, recombinant His6-tagged enzyme | Ostreococcus sp. 'lucimarinus' |