Literature summary 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.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.1.1.168	0.014	-	isatin	ketopantoyl lactone, enzyme form A	Saccharomyces cerevisiae
1.1.1.168	0.031	-	ketopantoyl lactone	enzyme form B	Saccharomyces cerevisiae
1.1.1.168	0.039	-	NADPH	enzyme form B	Saccharomyces cerevisiae
1.1.1.168	0.062	-	NADPH	enzyme form A	Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.1.1.168	27000	-	enzyme form A and B, gel filtration	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.1.1.168	2-dehydropantoyl lactone + NADPH	Saccharomyces cerevisiae	-	(R)-pantoyl lactone + NADP+	-	?

Organism

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

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.1.1.168	-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.168	2-dehydropantoyl lactone + NADPH	-	Saccharomyces cerevisiae	(R)-pantoyl lactone + NADP+	-	?
1.1.1.168	isatin + NADPH	-	Saccharomyces cerevisiae	?	-	?

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.1.1.168	5.1	5.6	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)