Literature summary for 1.1.1.22 extracted from

Sennett, N.C.; Kadirvelraj, R.; Wood, Z.A.
Conformational flexibility in the allosteric regulation of human UDP-alpha-D-glucose 6-dehydrogenase (2011), Biochemistry, 50, 9651-9663.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
2.3 A resolution crystal structure of the deletion construct DELTA132 reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the deletion construct as a hexamer with point group symmetry 32, similar to that of the active complex. In contrast, the UDP-alpha-D-xylose-inhibited enzyme forms a lower-symmetry, horseshoe-shaped hexameric complex. The DELTA132 and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces	Homo sapiens

Crystallization (Comment)

Organism

2.3 A resolution crystal structure of the deletion construct DELTA132 reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the deletion construct as a hexamer with point group symmetry 32, similar to that of the active complex. In contrast, the UDP-alpha-D-xylose-inhibited enzyme forms a lower-symmetry, horseshoe-shaped hexameric complex. The DELTA132 and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
DELTA132	deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
UDP-alpha-D-xylose	competitive. The DELTA132 deletion mutant and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces, suggesting that the hinge-bending motion represents a path for the allosteric transition between the different hexameric states	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60701	-	-

Synonyms

Synonyms	Comment	Organism
UGDH	-	Homo sapiens