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Alpha-N-acetylgalactosaminidase
α-N-acetylgalactosaminidaseEC 3.2.1.49 is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA (gene), NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Enzymes with this activity is useful for converting type A blood to type O, giving it the name of A-zyme. Bacterial enzymes in the GH109 family, including the A-zyme from ''Elizabethkingia meningoseptica'', runs this reaction efficiently. Nagalase catalyzes the deglycosylation of the Gc protein also known as vitamin D3 binding protein (VDBP) rendering it incapable of being converted to the regulatory protein, Gc Macrophage Activating Factor (GcMAF). GcMAF is a protein involved in the activation of macrophages - in cases when many types of incompatible cells happen to be around, thus nagalase diminishes the body’s macrophage activating capacity, and elevated naga ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NAGA (gene)
Alpha-N-acetylgalactosaminidase is an enzyme that in humans is encoded by the ''NAGA'' gene. NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. Mutations in NAGA have been identified as the cause of Schindler disease types I and II (type II also known as Kanzaki disease Kanzaki may refer to: Places *Kanzaki, Saga, a city in Saga Prefecture, Japan *Kanzaki, Hyōgo, a former town in Kanzaki District, Hyōgo Prefecture, Japan *Kanzaki District (other), multiple districts in Japan *Kanzaki Station (disambigua ...). References Further reading * * * * * * * * * * * * * * * * * * * External links * Human proteins {{gene-22-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Schindler Disease
Schindler disease, also known as Kanzaki disease and alpha-N-acetylgalactosaminidase deficiency is a rare disease found in humans. This lysosomal storage disorder is caused by a deficiency in the enzyme alpha-NAGA ( alpha-N-acetylgalactosaminidase), attributable to mutations in the NAGA gene on chromosome 22, which leads to excessive lysosomal accumulation of glycoproteins. A deficiency of the alpha-NAGA enzyme leads to an accumulation of glycosphingolipids throughout the body. This accumulation of sugars gives rise to the clinical features associated with this disorder. Schindler disease is an autosomal recessive disorder, meaning that one must inherit an abnormal allele from both parents in order to have the disease. Types There are three main types of the disease each with its own distinctive symptoms. ''Type I'' infantile form, infants will develop normally until about a year old. At this time, the affected infant will begin to lose previously acquired skills involving the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase
Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Occurrence and importance Glycoside hydrolases are found in essentially all domains of life. In prokaryotes, they are found both as intracellular and extracellular enzymes that are largely involved in nutrient acquisition. One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Type A Blood
The ABO blood group system is used to denote the presence of one, both, or neither of the A and B antigens on erythrocytes. For human blood transfusions, it is the most important of the 43 different blood type (or group) classification systems currently recognized by the International Society of Blood Transfusions (ISBT) as of June 2021. A mismatch (very rare in modern medicine) in this, or any other serotype, can cause a potentially fatal adverse reaction after a transfusion, or an unwanted immune response to an organ transplant. The associated anti-A and anti-B antibodies are usually IgM antibodies, produced in the first years of life by sensitization to environmental substances such as food, bacteria, and viruses. The ABO blood types were discovered by Karl Landsteiner in 1901; he received the Nobel Prize in Physiology or Medicine in 1930 for this discovery. ABO blood types are also present in other primates such as apes and Old World monkeys. History Discovery The ABO bl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Elizabethkingia Meningoseptica
''Elizabethkingia meningoseptica'' is a Gram-negative, rod-shaped bacterium widely distributed in nature (e.g. fresh water, salt water, or soil). It may be normally present in fish and frogs; it may be isolated from chronic infectious states, as in the sputum of cystic fibrosis patients. In 1959, American bacteriologist Elizabeth O. King (who isolated ''Kingella kingae'' in 1960) was studying unclassified bacteria associated with pediatric meningitis at the Centers for Disease Control and Prevention in Atlanta, when she isolated an organism (CDC group IIa) that she named ''Flavobacterium meningosepticum'' (''Flavobacterium'' means "the yellow bacillus" in Latin; ''meningosepticum'' likewise means "associated with meningitis and sepsis"). In 1994, it was reclassified in the genus ''Chryseobacterium'' and renamed ''Chryseobacterium meningosepticum''(''chryseos'' = "golden" in Greek, so ''Chryseobacterium'' means a golden/yellow rod similar to ''Flavobacterium''). In 2005, a 16S ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
