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Literature summary for 1.2.7.1 extracted from

  • Zhou, Z.H.; Adams, M.W.
    Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions (1997), Biochemistry, 36, 10892-10900.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + 2 oxidized ferredoxin the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys Pyrococcus furiosus acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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 ?

Synonyms

Synonyms Comment Organism
POR
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 Pyrococcus furiosus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information pH 8.0, 80°C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin Pyrococcus furiosus