An alpha-galactosidase A that is encoded in the genome of human. [PRO:DNx, UniProtKB:P06280]
EC 3.2.1.22;
Alpha-D-galactosidase A;
Alpha-D-galactoside galactohydrolase;
Galactosylgalactosylglucosylceramidase GLA;
3.2.1.47;
Melibiase
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 2 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| 1-deoxynojirimycin | Homo sapiens (human) | Ki | 18.0000 | 1 | 1 |
| migalastat | Homo sapiens (human) | IC50 | 0.0488 | 4 | 4 |
This protein enables 7 target(s):
| Target | Category | Definition |
|---|---|---|
| catalytic activity | molecular function | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. [GOC:vw, ISBN:0198506732] |
| alpha-galactosidase activity | molecular function | Catalysis of the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. [EC:3.2.1.22] |
| signaling receptor binding | molecular function | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:bf, GOC:ceb, ISBN:0198506732] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| hydrolase activity | molecular function | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. [ISBN:0198506732] |
| galactoside binding | molecular function | Binding to a glycoside in which the sugar group is galactose. [GOC:jl, ISBN:0198506732] |
| protein homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|---|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
| Golgi apparatus | cellular component | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732] |
| azurophil granule lumen | cellular component | The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid. [GOC:bf, PMID:17152095] |
| lysosomal lumen | cellular component | The volume enclosed within the lysosomal membrane. [GOC:jl, PMID:15213228] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|---|---|
| oligosaccharide metabolic process | biological process | The chemical reactions and pathways involving oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. [ISBN:0198506732] |
| negative regulation of nitric oxide biosynthetic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide. [GOC:go_curators] |
| glycosylceramide catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of glycosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of a monosaccharide (or derivative) by a ceramide group. [GOC:ai] |
| glycosphingolipid catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide. [ISBN:0198506732] |
| negative regulation of nitric-oxide synthase activity | biological process | Any process that stops or reduces the activity of the enzyme nitric-oxide synthase. [GOC:ai] |
| glycoside catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of glycosides, compounds in which a glycosyl group is substituted into a hydroxyl, thiol or selenol group in another compound. [GOC:go_curators] |