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Literature summary for 1.1.1.168 extracted from

  • King, H.L.; Dyar, R.E.; Wilken, D.R.
    Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase (1974), J. Biol. Chem., 249, 4689-4695.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
 isatin ketopantoyl lactone, enzyme form A Saccharomyces cerevisiae
0.031
-
 ketopantoyl lactone enzyme form B Saccharomyces cerevisiae
0.039
-
 NADPH enzyme form B Saccharomyces cerevisiae
0.062
-
 NADPH enzyme form A Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
 enzyme form A and B, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-dehydropantoyl lactone + NADPH Saccharomyces cerevisiae
-
 (R)-pantoyl lactone + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 2 enzyme forms: A and B with similar properties
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-dehydropantoyl lactone + NADPH
-
 Saccharomyces cerevisiae (R)-pantoyl lactone + NADP+
-
 ?
isatin + NADPH
-
 Saccharomyces cerevisiae ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1 5.6
-
 Saccharomyces cerevisiae