EC Number |
Application |
Reference |
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2.7.7.13 | agriculture |
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 |
2.7.7.13 | drug development |
the enzyme is a potential target for antimicrobial drug design, i.e. in the treatment of cystic fibrosis caused by Burkholderia cenocepacia |
690577 |
2.7.7.13 | drug development |
the enzyme is a target for inhibitor design for anti-leishmanial therapy |
723331 |
2.7.7.13 | medicine |
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 |
2.7.7.13 | medicine |
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 |
2.7.7.13 | medicine |
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 |
2.7.7.13 | synthesis |
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 |
2.7.7.13 | synthesis |
enzyme can be used for the synthesis of GDPmannose deoxy derivatives |
642876 |