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Literature summary for 2.7.7.9 extracted from

  • Decker, D.; Meng, M.; Gornicka, A.; Hofer, A.; Wilczynska, M.; Kleczkowski, L.A.
    Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase (2012), Phytochemistry, 79, 39-45.
    View publication on PubMed
Search for more literature for 2.7.7.9

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hordeum vulgare

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics, overview Hordeum vulgare
0.025
-
 UTP pH 7.5, temperature not specified in the publication Hordeum vulgare
0.033
-
 alpha-D-glucose 1-phosphate pH 7.5, temperature not specified in the publication Hordeum vulgare
10
-
 alpha-D-galactose 1-phosphate pH 7.5, temperature not specified in the publication Hordeum vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + alpha-D-glucose 1-phosphate Hordeum vulgare
-
 diphosphate + UDP-glucose
-
 r

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Hordeum vulgare
-
root
-
 Hordeum vulgare
-
seed developing seeds Hordeum vulgare
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyses a freely reversible reaction and is specific for alpha-D-glucose 1-phosphate Hordeum vulgare ?
-
 ?
UTP + alpha-D-galactose 1-phosphate low activity Hordeum vulgare diphosphate + UDP-galactose
-
 r
UTP + alpha-D-glucose 1-phosphate
-
 Hordeum vulgare diphosphate + UDP-glucose
-
 r

Subunits

Subunits Comment Organism
dimer inactive enzyme form Hordeum vulgare
monomer active enzyme form Hordeum vulgare
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

Synonyms

Synonyms Comment Organism
UDP-Glc pyrophosphorylase
-
 Hordeum vulgare
UDP-glucose pyrophosphorylase
-
 Hordeum vulgare
UGPase
-
 Hordeum vulgare

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8.5 broad optimum in both reaction directions Hordeum vulgare

pH Range

pH Minimum pH Maximum Comment Organism
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
5.5 9.5 reverse reaction, inactive above pH 10.0 and below pH 5.0, profile overview Hordeum vulgare

General Information

General Information Comment Organism
evolution the plant UGPases belongs to the so called UGPase-A family Hordeum vulgare
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
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