Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.9 extracted from

  • Fuehring, J.; Damerow, S.; Fedorov, R.; Schneider, J.; Muenster-Kuehnel, A.K.; Gerardy-Schahn, R.
    Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase (2013), Glycobiology, 23, 426-437.
    View publication on PubMed
Search for more literature for 2.7.7.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of the N-terminally StrepII-tagged enzyme in Escherichia coli BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
H446S site-directed mutagenesis, the mutant shows only slight dissociation and slightly reduced activity in forward and reverse reactionsactivity Homo sapiens
H497A site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions Homo sapiens
H497A site-directed mutagenesis, the mutant shows only slight dissociation and retains full activity in the reverse eaction, but shows reduced reaction in the forward reaction Homo sapiens
I466T site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions Homo sapiens
I468K site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, the mutant shows reduced activity in the reverse reaction Homo sapiens
I487D site-directed mutagenesis, the mutant shows dissociation of subunits, and highly reduced activity in forward and reverse reactions Homo sapiens
L492E site-directed mutagenesis, the mutant shows only slight dissociation and retains activity Homo sapiens
additional information truncation mutant DELTA 490-497 is almost inactive due to dissociation into di- and monomers Homo sapiens
N391P/L492E site-directed mutagenesis, inactive mutant showing dissociation into di- and monomers Homo sapiens
N491P site-directed mutagenesis, the mutant shows reduced activity in the reverse reaction Homo sapiens
T448K site-directed mutagenesis, the mutant shows dissociation of subunits, a tetramer appears in addition to di- and monomers, and highly reduced activity in forward and reverse reactions Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
423700
-
 gel filtration, recombinant enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally StrepII-tagged enzyme from Escherichia coli BL21(DE3) by affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + alpha-D-glucose 1-phosphate
-
 Homo sapiens diphosphate + UDP-glucose
-
 r

Subunits

Subunits Comment Organism
More structure-function relationships analysis, overview Homo sapiens
octamer octamers are formed by contacts between highly conserved amino acids in the C-terminal beta-helix Homo sapiens

Synonyms

Synonyms Comment Organism
UDP-glucose pyrophosphorylase
-
 Homo sapiens
UGP
-
 Homo sapiens
uridine diphosphate-glucose pyrophosphorylase
-
 Homo sapiens

General Information

General Information Comment Organism
evolution a feature that discriminates UGPs of different species is the quaternary organization. While UGPs in protists are monomers, di- and tetrameric forms exist in bacteria, and the enzyme from yeast and human are octameric UGPs Homo sapiens
additional information hUGPs are active in the octameric state and do not dissociate during the enzymatic cycle, structure-function relationships analysis, overview Homo sapiens