1.1.1.214: 2-dehydropantolactone reductase (Si-specific)
This is an abbreviated version!
For detailed information about 2-dehydropantolactone reductase (Si-specific), go to the full flat file.
Reaction
Synonyms
2-dehydropantoyl-lactone reductase (B-specific), 2-ketopantoyl lactone reductase, 2-oxopantoyl lactone reductase, conjugated polyketone reductase, conjugated polyketone reductase C2, CORT_0G03830, CPR, CPR-C1, CPR-C2, ketopantoyl lactone reductase, NADPH-dependent conjugated polyketone reductase, NADPH-dependent ketopantoyl lactone reductase, nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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Substrates Products
Substrates Products on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific)
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REACTION DIAGRAM
keto-omega-methylpantoyl lactone + NADPH
methylpantoyl lactone + NADP+
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the only compound other than ketopantoyl lactone which is a substrate, 73% relative activity to ketopantoyl lactone with form A enzyme, 56% relative activity to ketopantoyl lactone with form B enzyme
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?
2-dehydropantolactone + NADPH
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-
-
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
i.e. ketopantoyl lactone
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-
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
i.e. ketopantoyl lactone
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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-
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?
2-dehydropantolactone + NADPH + H+
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-
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
-
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
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r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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-
-
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?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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-
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?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
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-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
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-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
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-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
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-
r
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
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the enzyme is involved in pantothenate biosynthesis, pantoyl lactone, the putative product of the reaction, together with beta-alanine and ATP are the substrate of pantothenate synthase
?
?
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structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
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?
additional information
?
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the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
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-
?
additional information
?
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structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
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-
?
additional information
?
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structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
-
-
?
additional information
?
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the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
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-
?
additional information
?
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the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
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-
?
additional information
?
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both forms of the enzyme are B-specific, the enzyme exhibits opposite stereospecificity from that observed with the Saccharomyces cerevisiae enzyme, which is A-specific, less than 5% relative activity to ketopantoyl lactone with the following 2-keto-gamma-lactones: 2-keto-4-hydroxy-3-methylbutyric acid-gamma-lactone, 2-keto-4-hydroxybutyric acid-gamma-lactone
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?
additional information
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the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
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