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Literature summary extracted from

  • Chen, P.Y.; Li, B.; Drennan, C.L.; Elliott, S.J.
    A reverse TCA cycle 2-oxoacid ferredoxin oxidoreductase that makes C-C bonds from CO2 (2019), Joule, 3, 595-611 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.7.3 expression in Escherichia coli Magnetococcus marinus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.7.3 structure of both native and substrate-bound forms, to 1.94 and 2.8 A resolution, respectively Magnetococcus marinus

Protein Variants

EC Number Protein Variants Comment Organism
1.2.7.3 E45Q mutation in subunit alpha, residue forms second coordination sphere interactions with Arg63 of subunit beta. Mutant has a lower KM for 2-oxoglutarate than wild-type while kcat is diminished Magnetococcus marinus
1.2.7.3 Y436F mutation in subunit alpha, residue forms second coordination sphere interactions with Arg63 of subunit beta. Mutant has a lower KM for 2-oxoglutarate than wild-type while kcat is diminished Magnetococcus marinus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.7.3 0.64
-
 2-oxoglutarate mutant E45Q, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 0.97
-
 2-oxoglutarate wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 1.3
-
 reduced ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 1.8
-
 oxidized ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 1.8
-
 2-oxoglutarate mutant Y436F, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 4.4
-
 2-oxoglutarate wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 4.9
-
 2-oxoglutarate wild-type, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 6.8
-
 CoA wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 10
-
 CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 32
-
 succinyl-CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.3 Magnetococcus marinus A0L8G4 and A0L8G5 A0L8G4 i.e. pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, A0L8G5 i.e. beta subunit
-
1.2.7.3 Magnetococcus marinus MC-1 A0L8G4 and A0L8G5 A0L8G4 i.e. pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, A0L8G5 i.e. beta subunit
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.3 2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
 Magnetococcus marinus succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 r
1.2.7.3 2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
 Magnetococcus marinus MC-1 succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 r
1.2.7.3 additional information enzyme is both CO2-fixing and 2-oxoglutarate oxidizing. Negligible activity with other 2-oxoacids, including glyoxylate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, 3-methyl-2-oxovalerate, phenylpyruvate and oxaloacetate and 2-oxoadipate Magnetococcus marinus ?
-
-
1.2.7.3 additional information enzyme is both CO2-fixing and 2-oxoglutarate oxidizing. Negligible activity with other 2-oxoacids, including glyoxylate, pyruvate, 2-oxobutyrate, 2-oxoisovalerate, 3-methyl-2-oxovalerate, phenylpyruvate and oxaloacetate and 2-oxoadipate Magnetococcus marinus MC-1 ?
-
-
1.2.7.3 succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 Magnetococcus marinus 2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
 ?
1.2.7.3 succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
 Magnetococcus marinus MC-1 2-oxoglutarate + CoA + 2 oxidized ferredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.7.3 Mmc1_1749 gene name, pyruvate flavodoxin/ferredoxin oxidoreductase domain protein Magnetococcus marinus
1.2.7.3 Mmc1_1750 gene name, beta subunit Magnetococcus marinus
1.2.7.3 OGOR
-
 Magnetococcus marinus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.7.3 0.45
-
 succinyl-CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 0.51
-
 reduced ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 6.8
-
 2-oxoglutarate mutant E45Q, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 10.8
-
 2-oxoglutarate wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 11.2
-
 CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 12.3
-
 oxidized ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 17.8
-
 2-oxoglutarate mutant Y436F, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 22.2
-
 2-oxoglutarate wild-type, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 24.7
-
 CoA wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 30.3
-
 2-oxoglutarate wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.7.3 8.5 10.5
-
 Magnetococcus marinus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.3 [4Fe-4S]-center protein contains 3.6 mol of iron and 3.4 mol of sulfur per mol of alphabeta heterodimer Magnetococcus marinus

General Information

EC Number General Information Comment Organism
1.2.7.3 physiological function OGOR operates bidirectionally, both CO2-fixing and 2-oxoglutarate oxidizing, and only ferredoxin Fd1 supports efficient catalysis. Residue Glu45alpha is a mobile residue that impacts catalytic bias toward CO2-fixation although it makes no direct contact with TPP-bound intermediates Magnetococcus marinus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.7.3 4.5
-
 2-oxoglutarate wild-type, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 6.9
-
 2-oxoglutarate wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 9.9
-
 2-oxoglutarate mutant Y436F, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 11
-
 2-oxoglutarate wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 11
-
 2-oxoglutarate mutant E45Q, pH 7.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 14
-
 succinyl-CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 390
-
 reduced ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 1100
-
 CoA wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 3600
-
 CoA wild-type, pH 8.5, temperature not specified in the publication Magnetococcus marinus
1.2.7.3 6800
-
 oxidized ferredoxin wild-type, pH 7.0, temperature not specified in the publication Magnetococcus marinus