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Literature summary extracted from

  • Qu, C.; Akanuma, S.; Tanaka, N.; Moriyama, H.; Oshima, T.
    Design, X-ray crystallography, molecular modelling and thermal stability studies of mutant enzymes at site 172 of 3-isopropylmalate dehydrogenase from Thermus thermophilus (2001), Acta Crystallogr. Sect. D, 57, 225-232.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.85 mutant enzymes A172V, A172G and A172F. As in the case of A172L enzyme, the A172F mutant can not be crystallized by the salting-out technique with ammonium sulfate. The crystal is obtained at pH 4.8 using polyethylene glycol 4000 as a precipitant. Crystals of mutant enzyme A172E are obtained from a drop equilibrated with reservoir solution consisting of 0.8 M ammonium sulfate pH 6.0 at either 15°C or 20°C K. Two types of crystals: one hexagonal bipyramidal and the other is tetragonal Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.85 A172D melting temperature is reduced by 2.7°C compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172F mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172F melting temperature is increased by 1.8°C compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172G melting temperature is reduced by 0.3°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme Thermus thermophilus
1.1.1.85 A172I melting temperature is increased by 2°C compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172L mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172L melting temperature is increased by 3°C compared to wild-type enzyme Thermus thermophilus
1.1.1.85 A172V melting temperature is increased by 1°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.85 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+
-
 Thermus thermophilus 2-oxoisocaproate + NADH + H+ + CO2
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.85 additional information
-
-
 Thermus thermophilus
1.1.1.85 61
-
 midpoint of thermal unfolding curve, mutant enzyme A172D Thermus thermophilus
1.1.1.85 64
-
 midpoint of thermal unfolding curve, mutant enzyme A172G Thermus thermophilus
1.1.1.85 65
-
 midpoint of thermal unfolding curve, mutant enzyme A172V Thermus thermophilus
1.1.1.85 66
-
 midpoint of thermal unfolding curve, mutant enzyme A172I and A172E Thermus thermophilus
1.1.1.85 67
-
 midpoint of thermal unfolding curve, mutant enzyme A172L and A172F Thermus thermophilus
1.1.1.85 87
-
 clear correlation was observed between the hyrophobicity and the thermostability of the enzyme Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.85 NAD+
-
 Thermus thermophilus