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Literature summary for 1.2.7.1 extracted from

  • Nishizawa, Y.; Yabuki, T.; Fukuda, E.; Wakagi, T.
    Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1 (2005), FEBS Lett., 579, 2319-2322.
    View publication on PubMed
Search for more literature for 1.2.7.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, enzyme Ape2126/2128 Aeropyrum pernix

Inhibitors

Inhibitors Comment Organism Structure
KCl 10–20% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 46–65% activation is reached, and further increased concentrations of KCl are inhibitory, enzyme Ape2126/2128 Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
 pyruvate pH 8.5, 80°C, enzyme Ape2126/2128 Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34936
-
 1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128 Aeropyrum pernix
35000
-
 1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128 Aeropyrum pernix
71639
-
 1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128 Aeropyrum pernix
72000
-
 1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128 Aeropyrum pernix
110000
-
 gel filtration, enzyme Ape2126/2128 Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YA13 and Q9YA11 Q9YA13: alpha-subunit, Q9YA11: beta-subunit
-

Purification (Commentary)

Purification (Comment) Organism
enzyme Ape2126/2128 Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-4-methyl-thio-butyrate + CoA + 2 methyl viologen enzyme Ape2126/2128, 37% of the activity compared to pyruvate Aeropyrum pernix ?
-
 ?
2-oxoadipate + CoA + 2 methyl viologen enzyme Ape2126/2128, 37% of the activity compared to pyruvate Aeropyrum pernix ?
-
 ?
2-oxobutyrate + CoA + 2 oxidized methyl viologen enzyme Ape2126/2128, 98% of the activity compared to pyruvate Aeropyrum pernix propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
 ?
glyoxylate + CoA + 2 oxidized methyl viologen enzyme Ape2126/2128, 89% of the activity compared to pyruvate Aeropyrum pernix ?
-
 ?
hydroxypyruvate + CoA + 2 methyl viologen enzyme Ape2126/2128, 38% of the activity compared to pyruvate Aeropyrum pernix ?
-
 ?
additional information activity with 2-oxoglutarate is 6% compared to the activity with pyruvate. No activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape2126/2128, Aeropyrum pernix ?
-
 ?
pyruvate + CoA + 2 oxidized methyl viologen enzyme Ape2126/2128 Aeropyrum pernix acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 71639 + 1 * 34936, calculated from sequence, enzyme Ape2126/2128 Aeropyrum pernix
heterodimer 1 * 72000 + 1 * 35000, SDS-PAGE, enzyme Ape2126/2128 Aeropyrum pernix

Synonyms

Synonyms Comment Organism
Ape2126/2128 ordered locus name Aeropyrum pernix
OFOR
-
 Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 assay at Aeropyrum pernix
105
-
 enzyme Ape2126/2128 Aeropyrum pernix

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
80 110 80°C: 45% of maximal activity, 110°C: 95% of maximal activity, enzyme Ape2126/2128 Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 20 min, stable, enzyme Ape2126/2128 Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 enzyme Ape2126/2128 Aeropyrum pernix

pH Range

pH Minimum pH Maximum Comment Organism
6 10 pH 6.0: about 45% of maximal activity, pH 10.0: about 60% of maximal activity, enzyme Ape2126/2128 Aeropyrum pernix