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Literature summary for 2.7.7.9 extracted from

  • Kleczkowski, L.A.; Martz, F.; Wilczynska, M.
    Factors affecting oligomerization status of UDP-glucose pyrophosphorylase (2005), Phytochemistry, 66, 2815-2821.
    View publication on PubMed
Search for more literature for 2.7.7.9

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol increases wild-type activity by about 25% Hordeum vulgare

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hordeum vulgare

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: Tween-20 Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare Q43772
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Hordeum vulgare

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 similar activities of the wild-type UGPase in Tris, Hepes or Mops buffers. Half of the activity in 100 mM sodium phosphate. Compared with the wild-type UGPase the mutants KK127-128LL, C99S and LIV135-137NIN display reduced activities in all buffers. Hordeum vulgare

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + D-glucose-1-phosphate
-
 Hordeum vulgare diphosphate + UDP-glucose
-
 ?

Subunits

Subunits Comment Organism
oligomer SDS-PAGE. Incubation of wild-type UGPase with phosphate or Tris buffers promote oligomerization, whereas Mops and Hepes completely dissociate the oligomers to monomers. Similar buffer effects for mutants KK127-128LL and C99S, small buffer effects for mutant LIV135-137NIN Hordeum vulgare