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Arabidopsis thaliana Polyclonal UGP2 Primary Antibody for WB - ABIN2559390
Meng, Wilczynska, Kleczkowski: Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from Arabidopsis. in Biochimica et biophysica acta 2008
Show all 14 Pubmed References
Cow (Bovine) Polyclonal UGP2 Primary Antibody for WB - ABIN2783324
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
High UGP2 expression is associated with malignant pancreatic lesions.
This study provides clear evidence that the octameric state is a prerequisite for activity in the uridine diphosphate-glucose pyrophosphorylase.
The crystal structure was determined and shown to form octamers through end-to-end and side-by-side interactions. Mutagenesis studies showed that both dissociation of octamers and mutations of the latch loop can significantly affect the activity.
GYS1 regulation by HIF plays a central role in the hypoxic accumulation of glycogen, and hypoxia also upregulates the expression of UTP:glucose-1-phosphate urydylyltransferase (UGP2) and 1,4-alpha glucan branching enzyme (GBE1)
Studies characterize UGP2 and its promotor acivity and show its expression in liver and skeletal muscle.
UGP1 is a cell death regulator.
UGP1 and UGP2, are differentially expressed, with UGP1 being predominant. UGP1 is closely co-regulated with carbohydrate metabolism, late embryogenesis and seed loading, while UGP2 with stress response, fertilized flowers and photosynthetic genes. [UGP1]
AtUGP1 and AtUGP2 genes are functionally redundant and UGPase activity is essential for both vegetative and reproductive phases in Arabidopsis.
Comparison of molecular masses of UGPases from root and leaf extracts revealed that the root protein was slightly larger, suggesting a post-translational modification.
The identification of a novel gene, UDP-glucose pyrophosphorylase3 (UGP3), required for sulfolipid biosynthesis, is described.
The enzyme encoded by this gene is an important intermediary in mammalian carbohydrate interconversions. It transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. In liver and muscle tissue, UDP-glucose is a direct precursor of glycogen\; in lactating mammary gland it is converted to UDP-galactose which is then converted to lactose. The eukaryotic enzyme has no significant sequence similarity to the prokaryotic enzyme. Two transcript variants encoding different isoforms have been found for this gene.
UTP--glucose-1-phosphate uridylyltransferase 2
, UTP--glucose-1-phosphate uridylyltransferase
, UDP-glucose diphosphorylase
, UDP-glucose pyrophosphorylase 1
, UGPase 2
, UTP-glucose-1-phosphate uridyltransferase
, Uridyl diphosphate glucose pyrophosphorylase-1
, uridyl diphosphate glucose pyrophosphorylase 2
, uridindiphosphoglucosepyrophosphorylase 2
, UDP-glucose pyrophosphorylase 2
, UDP glucose pyrophosphorylase
, UDP-glucose pyrophosphorylase-like protein
, UTP:alpha-D-glucose-1-phosphate uridylyltransferase