Literature summary for 1.1.1.22 extracted from

Lee, H.S.; Son, Y.J.; Chong, S.H.; Bae, J.Y.; Leem, C.H.; Jang, Y.J.; Choe, H.
Computational analysis of the quaternary structural changes induced by point mutations in human UDP-glucose dehydrogenase (2009), Arch. Biochem. Biophys., 486, 35-43.

Search for more literature for 1.1.1.22

Crystallization (Commentary)

Crystallization (Comment)	Organism
the structure of UGDH in the crystal form reveals a hexameric arrangement, composed a trimer of dimers of six subunits	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A222Q/S233G	is a dimer in solution	Homo sapiens
C276A	is a hexamer-dimer mixture	Homo sapiens
C276S	is a hexamer	Homo sapiens
D280N	shows, exclusively, a hexameric quaternary structure in solution	Homo sapiens
K220A	shows, exclusively, a hexameric quaternary structure in solution	Homo sapiens
K279A	is essentially a dimer	Homo sapiens
K339A	is a dimer	Homo sapiens
additional information	perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60701	-	-

Synonyms

Synonyms	Comment	Organism
UDP-glucose dehydrogenase	-	Homo sapiens
UGDH	-	Homo sapiens

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Release 2023.1 (January 2023)