EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.22 | more |
the transient capacity to dissociate and reorganize the hydrogen bond network at the interface between dimeric units is an important element of the normal catalytic cycle |
Homo sapiens |
? |
- |
? |
1.1.1.22 | more |
thionicotinamide adenine dinucleotide |
Escherichia coli |
? |
- |
? |
1.1.1.22 | more |
thionicotinamide adenine dinucleotide |
Papiliotrema laurentii |
? |
- |
? |
1.1.1.22 | UDP-glucose + 2 NAD+ + H2O |
UDPGDH-A activity has a more important role than UDPGDH-B in synthesis of UDP-glucuronate |
Zea mays |
UDP-glucuronate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-alpha-D-glucose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-alpha-D-glucose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii DSM 3757 |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-alpha-D-mannose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii |
UDP-alpha-D-mannuronate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-alpha-D-mannose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii DSM 3757 |
UDP-alpha-D-mannuronate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-D-galactose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii |
UDP-alpha-D-galacturonate + 2 NADH + 2 H+ |
- |
? |
1.1.1.22 | UDP-D-galactose + 2 NAD+ + H2O |
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme |
Haloferax volcanii DSM 3757 |
UDP-alpha-D-galacturonate + 2 NADH + 2 H+ |
- |
? |