Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
NaCl | is able to function in a variety of salt concentrations, enzymatic activity improves as salinity decreases. At 4 M NaCl concentration the enzyme was able to produce 870 nM NADH, while at 0.5 M NaCl, over 1.5 mM NADH is produced | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | Haloferax volcanii | the enzyme is involved in protein N-glycosylation | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | Haloferax volcanii DSM 3757 | the enzyme is involved in protein N-glycosylation | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GYH5 | - |
- |
Haloferax volcanii DSM 3757 | D4GYH5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | the enzyme is involved in protein N-glycosylation | Haloferax volcanii | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
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+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | the enzyme is involved in protein N-glycosylation | Haloferax volcanii DSM 3757 | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
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+ | - |
? | |
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+ | - |
? | |
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+ | - |
? | |
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+ | - |
? | |
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+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AglM | - |
Haloferax volcanii |
HVO_1531 | locus name | Haloferax volcanii |
UDP-glucose dehydrogenase | - |
Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
malfunction | Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer | Haloferax volcanii |
physiological function | the enzyme is involved in protein N-glycosylation | Haloferax volcanii |