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Literature summary for 1.1.1.85 extracted from

  • Graczer, E.; Varga, A.; Melnik, B.; Semisotnov, G.; Zavodszky, P.; Vas, M.
    Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-isopropylmalate dehydrogenases (2009), Biochemistry, 48, 1123-1134.
    View publication on PubMed

Protein Variants

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

Metals/Ions Comment Organism Structure
Mg2+
-
Vibrio sp.
Mg2+
-
Escherichia coli
Mg2+
-
Thermus thermophilus

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Escherichia coli P30125
-
-
Thermus thermophilus Q5SIY4
-
-
Vibrio sp.
-
-
-
Vibrio sp. I5
-
-
-

Renatured (Commentary)

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 and Products (Substrate)

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

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

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

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