Literature summary for 1.1.1.22 extracted from

Grady, G.; Thelen, A.; Albers, J.; Ju, T.; Guo, J.; Barycki, J.J.; Simpson, M.A.
Inhibiting hexamer disassembly of human UDP-glucose dehydrogenase by photoactivated amino acid cross-linking (2016), Biochemistry, 55, 3157-3164 .

Search for more literature for 1.1.1.22

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant	Homo sapiens

General Stability

General Stability	Organism
wild-type UGDH is relatively stable to proteolysis in the apoenzyme form but is further stabilized by addition of NADH cofactor, UDP-glucose substrate, or a combination of the two to form a ternary enzyme complex	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120000	-	gel filtration, mutant containing 4-benzoyl-L-phenylalanine at position 96	Homo sapiens
360000	-	gel filtration, mutant containing 4-benzoyl-L-phenylalanine at position 458	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60701	-	-

Subunits

Subunits	Comment	Organism
dimer	and trimer and hexamer, 2 * 60000, SDS-PAGE	Homo sapiens
hexamer	and dimer and trimer, 6 * 60000, SDS-PAGE	Homo sapiens
trimer	and dimer and hexamer, 3 * 60000, SDS-PAGE	Homo sapiens

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Release 2023.1 (January 2023)