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Literature summary for 1.1.1.85 extracted from

  • Ohmae, E.; Hamajima, Y.; Nagae, T.; Watanabe, N.; Kato, C.
    Similar structural stabilities of 3-isopropylmalate dehydrogenases from the obligatory piezophilic bacterium Shewanella benthica strain DB21MT-2 and its atmospheric congener S. oneidensis strain MR-1 (2018), Biochim. Biophys. Acta Proteins Proteom., 1866, 680-691 .
    View publication on PubMed
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General Stability

General Stability Organism
at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa Shewanella benthica
at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa. The pressure-dependent activity does not originate from structural perturbations such as unfolding or dimer dissociation Shewanella oneidensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2R,3S)-3-isopropylmalate + NAD+ Shewanella benthica
-
 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir
(2R,3S)-3-isopropylmalate + NAD+ Shewanella oneidensis
-
 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir
(2R,3S)-3-isopropylmalate + NAD+ Shewanella benthica DB21MT-2
-
 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir

Organic Solvent Stability

Organic Solvent Comment Organism
urea urea-induced unfolding of the enzyme follows a three-state unfolding model, including a dimer intermediate. The first transition is strongly pH-dependent but pressure-independent. The second transition shows the opposite pattern Shewanella benthica
urea urea-induced unfolding of the enzyme follows a three-state unfolding model, including a dimer intermediate. The first transition is strongly pH-dependent but pressure-independent. The second transition shows the opposite pattern Shewanella oneidensis

Organism

Organism UniProt Comment Textmining
Shewanella benthica D2YZL2
-
-
Shewanella benthica DB21MT-2 D2YZL2
-
-
Shewanella oneidensis Q8E9N3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Shewanella benthica
-
 Shewanella oneidensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R,3S)-3-isopropylmalate + NAD+
-
 Shewanella benthica 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir
(2R,3S)-3-isopropylmalate + NAD+
-
 Shewanella oneidensis 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir
(2R,3S)-3-isopropylmalate + NAD+
-
 Shewanella benthica DB21MT-2 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ir

Synonyms

Synonyms Comment Organism
IPMDH
-
 Shewanella benthica

General Information

General Information Comment Organism
metabolism the enzyme is involved in leucine biosynthesis Shewanella benthica
metabolism the enzyme is involved in leucine biosynthesis Shewanella oneidensis