EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.9 | expression in Escherichia coli | Hordeum vulgare |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.9 | additional information | - |
additional information | kinetics, overview | Hordeum vulgare | |
2.7.7.9 | 0.025 | - |
UTP | pH 7.5, temperature not specified in the publication | Hordeum vulgare | |
2.7.7.9 | 0.033 | - |
alpha-D-glucose 1-phosphate | pH 7.5, temperature not specified in the publication | Hordeum vulgare | |
2.7.7.9 | 10 | - |
alpha-D-galactose 1-phosphate | pH 7.5, temperature not specified in the publication | Hordeum vulgare |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | Hordeum vulgare | - |
diphosphate + UDP-glucose | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.9 | Hordeum vulgare | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.9 | recombinant enzyme from Escherichia coli | Hordeum vulgare |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.7.9 | leaf | - |
Hordeum vulgare | - |
2.7.7.9 | root | - |
Hordeum vulgare | - |
2.7.7.9 | seed | developing seeds | Hordeum vulgare | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.9 | additional information | the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate | Hordeum vulgare | ? | - |
? | |
2.7.7.9 | UTP + alpha-D-galactose 1-phosphate | low activity | Hordeum vulgare | diphosphate + UDP-galactose | - |
r | |
2.7.7.9 | UTP + alpha-D-glucose 1-phosphate | - |
Hordeum vulgare | diphosphate + UDP-glucose | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.7.9 | dimer | inactive enzyme form | Hordeum vulgare |
2.7.7.9 | monomer | active enzyme form | Hordeum vulgare |
2.7.7.9 | More | structure modeling, overview. The quaternary structure of the enzyme is affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity. The ratio of monomers to dimers is about 5:1 in absence of substrate | Hordeum vulgare |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.7.9 | UDP-Glc pyrophosphorylase | - |
Hordeum vulgare |
2.7.7.9 | UDP-glucose pyrophosphorylase | - |
Hordeum vulgare |
2.7.7.9 | UGPase | - |
Hordeum vulgare |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.9 | 6.5 | 8.5 | broad optimum in both reaction directions | Hordeum vulgare |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.9 | 4.5 | 10 | forward reaction sharp drop in activity above pH 10.0, inactive above pH 10.0 and below pH 4.0, profile overview | Hordeum vulgare |
2.7.7.9 | 5.5 | 9.5 | reverse reaction, inactive above pH 10.0 and below pH 5.0, profile overview | Hordeum vulgare |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.7.9 | evolution | the plant UGPases belongs to the so called UGPase-A family | Hordeum vulgare |
2.7.7.9 | additional information | structure modeling, overview. The quaternary structure of the enzyme is affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity | Hordeum vulgare |
2.7.7.9 | physiological function | UDP-Glc pyrophosphorylase is an essential enzyme responsible for production of UDP-Glc, which is used in hundreds of glycosylation reactions involving addition of Glc to a variety of compounds | Hordeum vulgare |