EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.169 | (S)-pantoate + NADP+ |
low activity |
Thermococcus kodakarensis |
2-dehydropantoate + NADPH + H+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADH + H+ |
- |
Thermococcus kodakarensis |
(R)-pantoate + NAD+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADH + H+ |
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes |
Thermococcus kodakarensis |
(R)-pantoate + NAD+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADH + H+ |
- |
Thermococcus kodakarensis ATCC BAA-918 |
(R)-pantoate + NAD+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADH + H+ |
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes |
Thermococcus kodakarensis ATCC BAA-918 |
(R)-pantoate + NAD+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADPH |
- |
Escherichia coli |
(R)-pantoate + NADP+ |
- |
? |
1.1.1.169 | 2-dehydropantoate + NADPH |
an essential step for the biosynthesis of pantothenate, i.e. vitamin B5 |
Escherichia coli |
(R)-pantoate + NADP+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADPH |
the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5 |
Escherichia coli |
(R)-pantoate + NADP+ |
- |
? |
1.1.1.169 | 2-dehydropantoate + NADPH |
substrate and product binding structures, hinge bending between the N- and C-terminal domains is observed, which triggers the switch of the essential Lys176 to form a key hydrogen bond with the C2 hydroxyl of pantoate, pantoate forms additional interactions with conserved residues Ser244, Asn98, and Asn180 and with two conservatively varied residues, Asn194 and Asn241, overview |
Escherichia coli |
(R)-pantoate + NADP+ |
- |
r |
1.1.1.169 | 2-dehydropantoate + NADPH + H+ |
- |
Escherichia coli |
(R)-pantoate + NADP+ |
- |
? |