Protein Variants | Comment | Organism |
---|---|---|
W152F | site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation | Thermus thermophilus |
W152F/W195F | site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation | Thermus thermophilus |
W77F/W152F | site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation | Thermus thermophilus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Vibrio sp. | |
Mg2+ | - |
Escherichia coli | |
Mg2+ | - |
Thermus thermophilus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
73300 | - |
2 * 73300, sequence calculation | Thermus thermophilus |
76960 | - |
2 * 76960, sequence calculation | Vibrio sp. |
78780 | - |
2 * 78780, sequence calculation | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P30125 | - |
- |
Thermus thermophilus | Q5SIY4 | - |
- |
Vibrio sp. | - |
- |
- |
Vibrio sp. I5 | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
refolding mechanism of the homodimeric enzyme, dilution of the denatured protein, overview. Association of the two polypeptide chains occurs at the beginning of refolding | Vibrio sp. |
refolding mechanism of the homodimeric enzyme, dilution of the denatured protein, overview. Association of the two polypeptide chains occurs at the beginning of refolding | Escherichia coli |
refolding mechanism of the homodimeric enzyme, dilution of the denatured protein, overview. Association of the two polypeptide chains occurs at the beginning of refolding, overview | Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
threo-D-3-isopropylmalate + NAD+ | domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 | Vibrio sp. | ? | - |
? | |
threo-D-3-isopropylmalate + NAD+ | domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 | Escherichia coli | ? | - |
? | |
threo-D-3-isopropylmalate + NAD+ | domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 | Thermus thermophilus | ? | - |
? | |
threo-D-3-isopropylmalate + NAD+ | domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 | Vibrio sp. I5 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 73300, sequence calculation | Thermus thermophilus |
homodimer | 2 * 76960, sequence calculation | Vibrio sp. |
homodimer | 2 * 78780, sequence calculation | Escherichia coli |
More | three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview | Vibrio sp. |
More | three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview | Escherichia coli |
More | three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview | Thermus thermophilus |
Synonyms | Comment | Organism |
---|---|---|
IPMDH | - |
Vibrio sp. |
IPMDH | - |
Escherichia coli |
IPMDH | - |
Thermus thermophilus |
two-domain 3-isopropylmalate dehydrogenase | - |
Vibrio sp. |
two-domain 3-isopropylmalate dehydrogenase | - |
Escherichia coli |
two-domain 3-isopropylmalate dehydrogenase | - |
Thermus thermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Vibrio sp. |
7.6 | - |
assay at | Escherichia coli |
7.6 | - |
assay at | Thermus thermophilus |