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Literature summary extracted from

  • Sharma, R.; Sastry, G.N.
    Deciphering the dynamics of non-covalent interactions affecting thermal stability of a protein: molecular dynamics study on point mutant of Thermus thermophilus isopropylmalate dehydrogenase (2015), PLoS ONE, 10, e0144294.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.85 A172L the mutant shows improved thermal stability compared to the wild type enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+ Thermus thermophilus
-
 (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
 ?
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+ Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.85 Thermus thermophilus Q5SIY4
-
-
1.1.1.85 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SIY4
-
-

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 (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
 ?
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.85 IPMDH
-
 Thermus thermophilus
1.1.1.85 isopropylmalate dehydrogenase
-
 Thermus thermophilus
1.1.1.85 leuB
-
 Thermus thermophilus

Cofactor

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