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Literature summary 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

EC Number Protein Variants Comment Organism
1.1.1.85 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
1.1.1.85 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
1.1.1.85 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

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.85 73300
-
2 * 73300, sequence calculation Thermus thermophilus
1.1.1.85 76960
-
2 * 76960, sequence calculation Vibrio sp.
1.1.1.85 78780
-
2 * 78780, sequence calculation Escherichia coli

Organism

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.1.85 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.
1.1.1.85 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
1.1.1.85 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.85 threo-D-3-isopropylmalate + NAD+ domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 Vibrio sp. ?
-
?
1.1.1.85 threo-D-3-isopropylmalate + NAD+ domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 Escherichia coli ?
-
?
1.1.1.85 threo-D-3-isopropylmalate + NAD+ domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2 Thermus thermophilus ?
-
?
1.1.1.85 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

EC Number Subunits Comment Organism
1.1.1.85 homodimer 2 * 73300, sequence calculation Thermus thermophilus
1.1.1.85 homodimer 2 * 76960, sequence calculation Vibrio sp.
1.1.1.85 homodimer 2 * 78780, sequence calculation Escherichia coli
1.1.1.85 More three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview Vibrio sp.
1.1.1.85 More three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview Escherichia coli
1.1.1.85 More three-dimensional structure of IPMDH, analysis of subunit-subunit interactions, overview Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.85 IPMDH
-
Vibrio sp.
1.1.1.85 IPMDH
-
Escherichia coli
1.1.1.85 IPMDH
-
Thermus thermophilus
1.1.1.85 two-domain 3-isopropylmalate dehydrogenase
-
Vibrio sp.
1.1.1.85 two-domain 3-isopropylmalate dehydrogenase
-
Escherichia coli
1.1.1.85 two-domain 3-isopropylmalate dehydrogenase
-
Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.85 7.6
-
assay at Vibrio sp.
1.1.1.85 7.6
-
assay at Escherichia coli
1.1.1.85 7.6
-
assay at Thermus thermophilus