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Literature summary for 1.2.7.11 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 1.2.7.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, enzyme Ape1473/1472 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 Ape1473/1472 Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
 pyruvate pH 8.5, 80°C, enzyme Ape1473/1472 Aeropyrum pernix
0.5
-
 2-oxoglutarate pH 8.5, 80°C, enzyme Ape1473/1472 Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 1 * 67000 + 1 * 34000, SDS-PAGE, enzyme Ape1473/1472 Aeropyrum pernix
34410
-
 1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472 Aeropyrum pernix
67000
-
 1 * 67000 + 1 * 34000, SDS-PAGE, enzyme Ape1473/1472 Aeropyrum pernix
67405
-
 1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472 Aeropyrum pernix
100000
-
 gel filtration, enzyme Ape1473/1472 Aeropyrum pernix

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Aeropyrum pernix Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix ?
-
 ?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-

Purification (Commentary)

Purification (Comment) Organism
enzyme Ape1473/1472 Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-4-methylthiobutyrate + CoA + 2 methyl viologen enzyme Ape1473/1472, 48% of the activity compared to glyoxylate Aeropyrum pernix 3-methylthiopropanoyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
2-oxoadipate + CoA + 2 methyl viologen enzyme Ape1473/1472, 49% of the activity compared to glyoxylate Aeropyrum pernix glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
2-oxobutyrate + CoA + 2 oxidized methyl viologen enzyme Ape1473/1472, 97% of the activity compared to glyoxylate Aeropyrum pernix propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
 ?
2-oxoglutarate + CoA + 2 oxidized methyl viologen enzyme Ape1473/1472, 94% of the activity compared to glyoxylate Aeropyrum pernix succinyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
4-hydroxyphenylpyruvate + CoA + 2 methyl viologen enzyme Ape1473/1472, 16% of the activity compared to glyoxylate Aeropyrum pernix (4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
glyoxylate + CoA + 2 oxidized methyl viologen enzyme Ape1473/1472 Aeropyrum pernix formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
hydroxypyruvate + CoA + 2 methyl viologen enzyme Ape1473/1472, 55% of the activity compared to glyoxylate Aeropyrum pernix ?
-
 ?
additional information Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix Aeropyrum pernix ?
-
 ?
additional information no activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape1473/1472 Aeropyrum pernix ?
-
 ?
phenylpyruvate + CoA + 2 methyl viologen enzyme Ape1473/1472, 24% of the activity compared to glyoxylate Aeropyrum pernix phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
phenylpyruvate + CoA + 2 methyl viologen enzyme Ape1473/1472, 36% of the activity compared to glyoxylate Aeropyrum pernix phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized methyl viologen enzyme Ape1473/1472, 95% of the activity compared to glyoxylate Aeropyrum pernix acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 67000 + 1 * 34000, SDS-PAGE, enzyme Ape1473/1472 Aeropyrum pernix
heterodimer 1 * 67405 + 1 * 34410, calculated from sequence, enzyme Ape1473/1472 Aeropyrum pernix

Synonyms

Synonyms Comment Organism
Ape1473/1472 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
110
-
 enzyme Ape1473/1472 Aeropyrum pernix

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
90 110 70°C: 17% of maximal activity, 90°C: about 40% of maximal activity, 110°C: maximal activity, enzyme Ape1473/1472 Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 20 min, stable, enzyme Ape1473/1472 Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 enzyme Ape1473/1472 Aeropyrum pernix

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10 pH 7.5: about 70% of maximal activity, pH 10.0: about 70% of maximal activity, enzyme Ape1473/1472 Aeropyrum pernix