EC |
1.1.1.168 |
Accepted name: |
2-dehydropantolactone reductase (Re-specific) |
Reaction: |
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+ |
Other name(s): |
2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific) |
Systematic name: |
(R)-pantolactone:NADP+ oxidoreductase (Re-specific) |
Comments: |
The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-75-9 |
References: |
1. |
King, H.L., Jr., Dyar, R.E. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689–4695. [PMID: 4603075] |
2. |
Wilken, D.R., King, H.L., Jr. and Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311–2314. [PMID: 234966] |
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[EC 1.1.1.168 created 1976, modified 1986, modified 1999] |
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