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Literature summary for 1.2.7.1 extracted from

  • Bock, A.; Kunow, J.; Glasemacher, J.; Schönheit, P.
    Catalytic properties, molecular composition and sequence alignments 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

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 pH 7, 37°C Methanosarcina barkeri
0.03
-
 oxidized ferredoxin clostridial ferredoxin, pH 7, 37°C Methanosarcina barkeri
0.07
-
 pyruvate pH 7, 37°C Methanosarcina barkeri
0.07
-
 Oxidized benzyl viologen clostridial ferredoxin, pH 7, 37°C Methanosarcina barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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 the enzyme is involved in catabolism of pyruvate acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin Methanosarcina barkeri DSM 804 the enzyme is involved in catabolism of pyruvate acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri P80521 and P80522 and P80523 and P80524 P80521: subunit PorA, P80522: subunit PorB, P80523: subunit PorC, P80524: subunit PorD
-
Methanosarcina barkeri DSM 804 P80521 and P80522 and P80523 and P80524 P80521: subunit PorA, P80522: subunit PorB, P80523: subunit PorC, P80524: subunit PorD
-

Oxidation Stability

Oxidation 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

Purification (Commentary)

Purification (Comment) Organism
-
 Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
-
 Methanosarcina barkeri propanoyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
2-oxobutyrate + CoA + 2 oxidized benzyl viologen
-
 Methanosarcina barkeri DSM 804 propanoyl-CoA + CO2 + 2 reduced benzyl viologen
-
 ?
additional information no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate Methanosarcina barkeri ?
-
 ?
additional information no oxidation of 2-oxoglutarate, indolepyruvate, phenylpyruvate, glyoxylate, 3-hydroxypyruvate and oxaloacetate Methanosarcina barkeri DSM 804 ?
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin the enzyme is involved in catabolism of pyruvate Methanosarcina barkeri acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin the deazaflavin, coenzyme F420, which has been proposed to be the physiological electron acceptor of pyruvate oxidoreductase in methanogens, is not reduced by the purified enzyme. In addition to ferredoxin and viologen dyes, flavin nucleotides serve as electron acceptors Methanosarcina barkeri acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin the enzyme is involved in catabolism of pyruvate Methanosarcina barkeri DSM 804 acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?
pyruvate + CoA + 2 oxidized ferredoxin the deazaflavin, coenzyme F420, which has been proposed to be the physiological electron acceptor of pyruvate oxidoreductase in methanogens, is not reduced by the purified enzyme. In addition to ferredoxin and viologen dyes, flavin nucleotides serve as electron acceptors Methanosarcina barkeri DSM 804 acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 ?

Subunits

Subunits Comment Organism
? alphabetagammadelta structure, 1 * 48000 (subunit PorA) + 1 * 30000 (subunit PorB) + 1 * 25000 (subunit PorC) + 1 * 15000 (subunit PorD), SDS-PAGE Methanosarcina barkeri

Synonyms

Synonyms Comment Organism
pyruvate:ferredoxin oxidoreductase
-
 Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Methanosarcina barkeri
59
-
-
 Methanosarcina barkeri

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 70 40°C: about 50% of maximal activity, 70°C: about 45% of maximal activity Methanosarcina barkeri

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
additional information FAD, FMN and lipoic acid are not found Methanosarcina barkeri
thiamine diphosphate the enzyme contained 1 mol/mol thiamine diphosphate Methanosarcina barkeri

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
10
-
 Sodium nitrite pH 7, 37°C Methanosarcina barkeri

General Information

General Information Comment Organism
metabolism the enzyme is involved in catabolism of pyruvate Methanosarcina barkeri