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Literature summary for 1.8.1.14 extracted from

  • Harris, D.R.; Ward, D.E.; Feasel, J.M.; Lancaster, K.M.; Murphy, R.D.; Mallet, T.C.; Crane, E.J., 3rd
    Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles (2005), FEBS J., 272, 1189-1200.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pyrococcus horikoshii

Reaction

Reaction Comment Organism Reaction ID
2 CoA + NADP+ = CoA-disulfide + NADPH + H+ mechanism Pyrococcus horikoshii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA-disulfide + NAD(P)H + H+ specific substrate Pyrococcus horikoshii CoA + NAD(P)+
-
 ?
additional information both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH, no substrate: dephospho-CoA Pyrococcus horikoshii ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.2
-
 NADPH 75°C Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
NADH both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH Pyrococcus horikoshii
NADPH both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH Pyrococcus horikoshii