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Literature summary extracted from

  • Kerscher, L.; Oesterhelt, D.
    Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium (1981), Eur. J. Biochem., 116, 587-594.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.2.7.11 the enzymes requires high salt concentrations for stability. The half-life at 0.1 M KCl in 50 mM Tris/HC1 pH 8.0 is 3 h at 0°C Halobacterium salinarum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.7.11 CoA substrate inhibition Halobacterium salinarum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.7.11 0.07
-
 2-oxobutyrate pH and temperature not specified in the publication Halobacterium salinarum
1.2.7.11 0.07
-
 oxidized ferredoxin cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication Halobacterium salinarum
1.2.7.11 0.07
-
 oxidized ferredoxin cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication Halobacterium salinarum
1.2.7.11 0.1
-
 pyruvate pH and temperature not specified in the publication Halobacterium salinarum
1.2.7.11 1.1
-
 2-oxoglutarate pH and temperature not specified in the publication Halobacterium salinarum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.11 Iron intact enzyme molecule contains two [4Fe-4S](2+,1+) clusters Halobacterium salinarum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.11 42000
-
 2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE Halobacterium salinarum
1.2.7.11 86000
-
 2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE Halobacterium salinarum
1.2.7.11 165000
-
 sedimentation velocity experiments Halobacterium salinarum

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.11 Halobacterium salinarum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.11
-
 Halobacterium salinarum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.11 2-oxobutyrate + CoA + oxidized ferredoxin
-
 Halobacterium salinarum propanoyl-CoA + CO2 + reduced ferredoxin
-
 ?
1.2.7.11 2-oxoglutarate + CoA + 2 oxidized ferredoxin specific activity under optimal conditions is 36% of the specific activity with 2-oxobutyrate Halobacterium salinarum succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
1.2.7.11 pyruvate + CoA + 2 oxidized ferredoxin specific activity under optimal conditions is 65% of the specific activity with 2-oxobutyrate Halobacterium salinarum acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.7.11 tetramer 2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE Halobacterium salinarum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.7.11 52
-
-
 Halobacterium salinarum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.7.11 25 52 the enzyme is twice as active at 52°C as at 25°C Halobacterium salinarum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.7.11 9
-
-
 Halobacterium salinarum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.7.11 8 9 pH 8.0: 65% of maximal activity, pH 9.0: optimum, inactive below pH 7.0 Halobacterium salinarum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.11 thiamine diphosphate intact enzyme molecule contains two molecules of thiamin diphosphate Halobacterium salinarum