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Literature summary for 2.7.7.9 extracted from

  • Fuehring, J.I.; Cramer, J.T.; Schneider, J.; Baruch, P.; Gerardy-Schahn, R.; Fedorov, R.
    A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism (2015), Sci. Rep., 5, 9618.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in the D4 octameric structure of the hUGP1-UDP-Glc complex, all subunits have the same overall conformation. The transition of the UGP octamer between the apo- and the product-bound forms is in agreement with the Monod-Wyman-Changeux symmetry model. oligomerzation facilitates an intermolecular stabilization of the sugar moiety in the active site (interlock mechanism), enhances protein stability, enables mild positive cooperativity observed for the octameric wild-type UGP1 towards diphosphate in the reverse reaction, and may allow regulation of the UGP octamer by modification of a single subunit Homo sapiens

Protein Variants

Protein Variants Comment Organism
D253L 0.063% of wild-type activity Homo sapiens
G115D 0.004% of wild-type activity Homo sapiens
G116A 0.067% of wild-type activity Homo sapiens
G222A insoluble protein Homo sapiens
H223L insoluble protein Homo sapiens
K127A 0.150% of wild-type activity Homo sapiens
K396A 0.041% of wild-type activity Homo sapiens
L113G insoluble protein Homo sapiens
N251L 0.011% of wild-type activity Homo sapiens
N328L insoluble protein Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16851
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-

Synonyms

Synonyms Comment Organism
UPD1 splicing variant Homo sapiens