Literature summary for 2.7.7.12 extracted from

McCorvie, T.J.; Kopec, J.; Pey, A.L.; Fitzpatrick, F.; Patel, D.; Chalk, R.; Shrestha, L.; Yue, W.W.
Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase (2016), Hum. Mol. Genet., 25, 2234-2244.

Application

Application	Comment	Organism
medicine	Q188R, the most commonly detected disease-associated variant, increases the rate of aggregation in the absence of zinc likely due to its reduced ability to form the uridylylated intermediate	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of ternary complex reveals a homodimer arrangement that contains a covalent uridylylated intermediate and glucose 1-phosphate in the active site, as well as a structural zinc-binding site, per monomer. Both uridylylation and zinc binding influence the stability and aggregation tendency of human GALT. Q188R, the most commonly detected disease-associated variant, increases the rate of aggregation in the absence of zinc likely due to its reduced ability to form the uridylylated intermediate	Homo sapiens

Crystallization (Comment)

Organism

crystal structure of ternary complex reveals a homodimer arrangement that contains a covalent uridylylated intermediate and glucose 1-phosphate in the active site, as well as a structural zinc-binding site, per monomer. Both uridylylation and zinc binding influence the stability and aggregation tendency of human GALT. Q188R, the most commonly detected disease-associated variant, increases the rate of aggregation in the absence of zinc likely due to its reduced ability to form the uridylylated intermediate

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P07902	-	-

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Release 2023.1 (January 2023)