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Literature summary for 1.8.1.10 extracted from

  • Loewen, P.C.
    Identification of a coenzyme A--glutathione disulfide (DSI), a modified coenzyme A disulfide (DSII), and a NADPH-dependent coenzyme A--glutathione disulfide reductase in E. coli (1977), Can. J. Biochem., 55, 1019-1027.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CoA-glutathione + NADPH Escherichia coli metabolism of CoA-glutathione disulfide, role may be to replenish the CoA pool from CoAS-SG formed either chemically or enzymatically during cell growth, accumulation of CoAS-SG in vivo in spite of high enzyme levels indicates involvement of a control mechanism glutathione + CoA + NADP+
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 specific activity of enzyme in crude extract increases during growth from early log phase into stationary phase and during a shift from aerobic to anaerobic growth Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA-glutathione + NADPH substrate coenzyme A-glutathione mixed disulfide, CoAS-SG, is capable of binding one molecule of Fe3+ Escherichia coli glutathione + CoA + NADP+
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CoA-glutathione + NADPH metabolism of CoA-glutathione disulfide, role may be to replenish the CoA pool from CoAS-SG formed either chemically or enzymatically during cell growth, accumulation of CoAS-SG in vivo in spite of high enzyme levels indicates involvement of a control mechanism Escherichia coli glutathione + CoA + NADP+
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 ?

Cofactor

Cofactor Comment Organism Structure
NADPH NADPH-dependent Escherichia coli