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Literature summary for 1.2.7.1 extracted from

  • Bock, A.K.; Kunow, J.; Glasemacher, J.; Schönheit, P.
    Catalytic properties, molecular composition and sequence alignment of pyruvate:ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro) (1996), Eur. J. Biochem., 237, 35-44.
    View publication on PubMed
Search for more literature for 1.2.7.1

Activating Compound

Activating Compound Comment Organism Structure
phosphate the purified enzyme is slightly stimulated by high phosphate concentrations. Addition of 200 mM potassium (or sodium) phosphate stimulates the enzyme activity 3-4fold Methanosarcina barkeri

General Stability

General Stability Organism
the enzyme is extremely oxygen sensitive, losing 90% of its activity upon exposure to air for 1 h at 0°C Methanosarcina barkeri

Inhibitors

Inhibitors Comment Organism Structure
Sodium nitrite
-
 Methanosarcina barkeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
 CoA 37°C, pH 7.0 Methanosarcina barkeri
0.03
-
 oxidized ferredoxin 37°C, pH 7.0, ferredoxin from Clostridium pasteurianum Methanosarcina barkeri
0.07
-
 pyruvate 37°C, pH 7.0 Methanosarcina barkeri
0.07
-
 Oxidized benzyl viologen 37°C, pH 7.0 Methanosarcina barkeri

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains about 12 mol of non-heme iron per mol of enzyme Methanosarcina barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
 x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE Methanosarcina barkeri
25000
-
 x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE Methanosarcina barkeri
30000
-
 x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE Methanosarcina barkeri
48000
-
 x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE Methanosarcina barkeri
130000
-
 gel filtration Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + CoA + 2 oxidized ferredoxin Methanosarcina barkeri first enzyme of pyruvate catabolism acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin Methanosarcina barkeri DSM 804 first enzyme of pyruvate catabolism acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri P80521 and P80522 and P80523 and P80524 P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
-
Methanosarcina barkeri DSM 804 P80521 and P80522 and P80523 and P80524 P80521: subunit A, P80522: subunit B, P80523: subunit C, P80524: subunit D
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanosarcina barkeri

Storage Stability

Storage Stability Organism
-20°C, under N2, after addition of 20% (v/v) glycerol to each fraction, the enzyme activity remains nearly constant for several weeks Methanosarcina barkeri
4°C, storage results in a loss of 80% of the activity within 8 days Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxobutyrate + CoA + 2 oxidized benzyl viologen coenzyme F420 is not reduced by the purified enzyme Methanosarcina barkeri propanoyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen coenzyme F420 is not reduced by the purified enzyme Methanosarcina barkeri DSM 804 propanoyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
additional information the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate Methanosarcina barkeri ?
-
 ?
additional information the enzyme does not catalyze the oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate Methanosarcina barkeri DSM 804 ?
-
 ?
pyruvate + CoA + 2 oxidized benzyl viologen coenzyme F420 is not reduced by the purified enzyme Methanosarcina barkeri acetyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
pyruvate + CoA + 2 oxidized benzyl viologen coenzyme F420 is not reduced by the purified enzyme Methanosarcina barkeri DSM 804 acetyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin first enzyme of pyruvate catabolism Methanosarcina barkeri acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin ferredoxin from Clostridium pasteurianum Methanosarcina barkeri acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin first enzyme of pyruvate catabolism Methanosarcina barkeri DSM 804 acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin ferredoxin from Clostridium pasteurianum Methanosarcina barkeri DSM 804 acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?

Subunits

Subunits Comment Organism
? x * 48000 + x * 30000 + x * 25000 + x * 15000, SDS-PAGE Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
59
-
-
 Methanosarcina barkeri

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
43 71 43°C: about 55% of maximal activity, 71°C: about 5% of maximal activity Methanosarcina barkeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Methanosarcina barkeri

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate contains 1 mol thiamine diphosphate per mol of enzyme Methanosarcina barkeri

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
10
-
 Sodium nitrite 37°C, pH 7.0 Methanosarcina barkeri

General Information

General Information Comment Organism
physiological function first enzyme of pyruvate catabolism Methanosarcina barkeri