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Results 1 - 8 of 8
EC Number Application Commentary Reference
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13agriculture over-expression of isoform Gmp3 increases total L-ascorbic acid contents and enhances the tolerance to oxidative stress in tomato. Knock-down of Gmp3 significantly decreases L-ascorbic acid contents below the threshold level and alters the phenotype of tomato plants with lesions and further senescence 739463
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13drug development the enzyme is a potential target for antimicrobial drug design, i.e. in the treatment of cystic fibrosis caused by Burkholderia cenocepacia 690577
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13drug development the enzyme is a target for inhibitor design for anti-leishmanial therapy 723331
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13medicine mutations in GMPPB can result in muscular dystrophy variants with hypoglycosylated alpha--dystroglycan. Muscle biopsies of affected individuals and available fibroblasts display reduced alpha-dystroglycan glycosylation. Five of the identified missense mutations cause formation of aggregates in the cytoplasm or near membrane protrusions 741569
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13medicine mutations in guanosine diphosphate mannose diphosphorylase B (GMPPB) can result in muscular dystrophy variants with hypoglycosylated alpha-dystroglycan. Reduced alpha-dystroglycan glycosylation is found in the muscle biopsies of individuals suffering from congenital and limb-girdle muscular dystrophies and in available fibroblasts. Overexpression of wild-type GMPPB in fibroblasts from an affected individual partially restored glycosylation of alpha-dystroglycan. Wild-type GMPPB localizes to the cytoplasm, but five of the identified missense mutations cause formation of aggregates in the cytoplasm or near membrane protrusions 737417
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13medicine mutations in guanosine diphosphate mannose diphosphorylase GMPPB can result in muscular dystrophy variants with hypoglycosylated alpha-dystroglycan. Produkt GDP-mannose is required for O-mannosylation of proteins, including alpha-dystroglycan, and it is the substrate of cytosolic mannosyltransferases. In the muscle biopsies of affected individuals and in available fibroblasts, reduced alpha-dystroglycan glycosylation is found. Overexpression of wild-type GMPPB in fibroblasts from an affected individual partially restores glycosylation of alpha-dystroglycan. Whereas wild-type GMPPB localizes to the cytoplasm, five of the identified missense mutations cause formation of aggregates in the cytoplasm or near membrane protrusions 737417
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13synthesis an N-acetylhexosamine 1-kinase from Bifidobacterium infantis (NahK_15697), a guanosine 5'-diphosphate (GDP)-mannose pyrophosphorylase from Pyrococcus furiosus (PFManC), and an Escherichia coli inorganic pyrophosphatase (EcPpA) are used efficiently for a one-pot three enzyme synthesis of GDP-mannose, GDP-glucose, their derivatives, and GDP-talose from simple monosaccharides and derivatives in preparative scale 726089
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13synthesis enzyme can be used for the synthesis of GDPmannose deoxy derivatives 642876
Results 1 - 8 of 8