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This data from this study indicate the importance of UDP-D-galactose synthesis by UGE4 for the organization and function of endomembranes, especially TGN/EEs, which are a sorting station of the secretory and vacuolar pathways.
Rough mapping and whole-genome sequencing identified the mutant with altered localization of NIP5;1 as an allele of UDP-glucose 4-epimerase 4.
RHD1, a UDP-glucose-4-epimerase, is a likely target of root-specific negative regulation by ethylene and that loss of RHD1 function results in a heightened sensitivity of root tissues to both ethylene and auxin. [RHD1]
UGE2 and UGE4 influence growth and cell wall carbohydrate biosynthesis throughout the plant, UGE3 is specialized for pollen development, and UGE1 and UGE5 might act in stress situations.
These studies reveal a new link between hepatic GALE activity and whole-body glucose homeostasis via regulation of hepatic Tff3 expression.
results provide evidence that the Xbp1s/GalE pathway functions as a novel regulatory nexus connecting the UPR to the characteristic postprandial metabolic changes in hepatocytes.
Mutation in UDP-galactose-4'-epimerase gene is associated with UDP-galactose-4'-epimerase deficiency.
Data show the protein structure of GALE and its substrate binding and specificity. It is mutated in type III galactosemia. [review]
human UDP-galactose 4'-epimerase stability is increased by variants associated with type III galactosemia but decreased by substrate and cofactor binding
These data indicated a critical role of GALE in maintaining cartilage homeostasis, and suggested that GALE inhibition might contribute to OA progress.
GALE variants can be arranged into three groups depending on the severity of enzyme impairment.
P.K161N-hGALE causes its effects by abolishing an important interaction between the protein and the cofactor.
study of hGALE crystal structure and demonstration that residue 307 acts as a gatekeeper mediating substrate access to the hGALE active site
Resulst describe the relationship among UDP-galactose 4'-epimerase activity, substrate specificity, metabolic balance, and galactose sensitivity in mammalian cells.
Disease-causing mutations result in a variety of changes to the steady-state parameters. Mostly these are changes in turnover number, kcat. The ability to dimerize is not affected, but some mutants have increased sensitivity to protease digestion.
Subtle biochemical and metabolic abnormalities detected in patients expressing these GALE alleles likely reflect, at least in part, the reduced enzymatic activity of the encoded GALE proteins.
Our observations show that altered protein stability is due to misfolding and that loss or reduction of enzyme activity is responsible for the molecular defects underlying GALE-deficiency galactosemia.
This gene encodes UDP-galactose-4-epimerase which catalyzes two distinct but analogous reactions: the epimerization of UDP-glucose to UDP-galactose, and the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The bifunctional nature of the enzyme has the important metabolic consequence that mutant cells (or individuals) are dependent not only on exogenous galactose, but also on exogenous N-acetylgalactosamine as a necessary precursor for the synthesis of glycoproteins and glycolipids. Mutations in this gene result in epimerase-deficiency galactosemia, also referred to as galactosemia type 3, a disease characterized by liver damage, early-onset cataracts, deafness and mental retardation, with symptoms ranging from mild ('peripheral' form) to severe ('generalized' form). Multiple alternatively spliced transcripts encoding the same protein have been identified.
, UDP-glucose 4-epimerase
, UDP-galactose 4-epimerase
, UDP-glucose (37.7 kD) (1N569)
, UDP galactose-4'-epimerase
, galactose-4-epimerase, UDP-
, short chain dehydrogenase/reductase family 1E, member 1
, galactose-4-epimerase, UDP