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The enzyme fructose bisphosphatase (EC 3.1.3.11; systematic name D-fructose-1,6-bisphosphate 1-phosphohydrolase) catalyses the conversion of fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways:
Alpha-mannosidosis is a lysosomal storage disorder, first described by Swedish physician Okerman in 1967. In humans it is known to be caused by an autosomal recessive genetic mutation in the gene MAN2B1, located on chromosome 19, affecting the production of the enzyme alpha-D-mannosidase, resulting in its deficiency. Consequently, if both parents are carriers, there will be a 25% chance with each pregnancy that the defective gene from both parents will be inherited, and the child will develop the disease. There is a two in three chance that unaffected siblings will be carriers. In livestock alpha-mannosidosis is caused by chronic poisoning with swainsonine from locoweed.
A debranching enzyme is a molecule that helps facilitate the breakdown of glycogen, which serves as a store of glucose in the body, through glucosyltransferase and glucosidase activity. Together with phosphorylases, debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. This constitutes a major source of energy reserves in most organisms. Glycogen breakdown is highly regulated in the body, especially in the liver, by various hormones including insulin and glucagon, to maintain a homeostatic balance of blood-glucose levels. When glycogen breakdown is compromised by mutations in the glycogen debranching enzyme, metabolic diseases such as Glycogen storage disease type III can result.
α-Mannosidase is an enzyme involved in the cleavage of the α form of mannose. Its systematic name is α-D-mannoside mannohydrolase.
In enzymology, a phosphomannomutase is an enzyme that catalyzes the chemical reaction
In enzymology, a dextransucrase is an enzyme that catalyzes the chemical reaction
In enzymology, a dextrin dextranase is an enzyme that catalyzes the chemical reaction
In enzymology, an alternansucrase is an enzyme that catalyzes a chemical reaction that transfers an alpha-D-glucosyl residue from sucrose alternately to the 6- and 3-positions of the non-reducing terminal residue of an alpha-D-glucan, thereby creating a glucan with alternating alpha-1,6- and alpha-1,3-bonds. The name "alternan" was coined in 1982 for the glucan based on its alternating linkage structure.
In enzymology, a sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase is an enzyme that catalyzes the chemical reaction
Epididymis-specific alpha-mannosidase is an enzyme that in humans is encoded by the MAN2B2 gene.
In molecular biology, glycoside hydrolase family 92 is a family of glycoside hydrolases.
Alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:6-(2- -alpha-D-mannosyl)-glycoprotein 6-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction
Beta-mannosylphosphodecaprenol---mannooligosaccharide 6-mannosyltransferase is an enzyme with systematic name beta-D-mannosylphosphodecaprenol:(1->6)-alpha-D-mannosyloligosaccharide 6-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction
Mannan 1,2-(1,3)-α-mannosidase is an enzyme with systematic name (1→2)-(1→3)-α-D-mannan mannohydrolase. It catalyses the hydrolysis of (1→2)- and (1→3)-linkages in yeast mannan, releasing mannose.
Mannan endo-1,6-α-mannosidase is an enzyme with systematic name 6-α-D-mannan mannanohydrolase. It catalyses the random hydrolysis of (1→6)-α-D-mannosidic linkages in unbranched (1→6)-mannans
Mannosyl-oligosaccharide 1,2-α-mannosidase (EC 3.2.1.113, mannosidase 1A, mannosidase 1B, 1,2-α-mannosidase, exo-α-1,2-mannanase, mannose-9 processing α-mannosidase, glycoprotein processing mannosidase I, mannosidase I, Man9-mannosidase, ManI, 1,2-α-mannosyl-oligosaccharide α-D-mannohydrolase) is an enzyme with systematic name 2-α-mannosyl-oligosaccharide α-D-mannohydrolase. It catalyses the hydrolysis of the terminal (1→2)-linked α-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Mannosyl-oligosaccharide 1,3-1,6-α-mannosidase (EC 3.2.1.114, mannosidase II, exo-1,3-1,6-α-mannosidase, α-D-mannosidase II, α-mannosidase II, α-3,6-mannosidase, GlcNAc transferase I-dependent α1,3[α1,6]mannosidase, Golgi α-mannosidase II, ManII, 1,3(1,6)-α-D-mannosidase, 1,3-(1,6-)mannosyl-oligosaccharide α-D-mannohydrolase) is an enzyme with systematic name (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase. It catalyses the hydrolysis of the terminal (1→3)- and (1→6)-linked α-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.
Glycoprotein endo-α-1,2-mannosidase (EC 3.2.1.130, glucosylmannosidase, endo-α-D-mannosidase, endo-α-mannosidase, endomannosidase, glucosyl mannosidase) is an enzyme with systematic name glycoprotein glucosylmannohydrolase. It catalyses the hydrolysis of the terminal α-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of the glycoprotein produced in the Golgi membrane.
Mannan exo-1,2-1,6-alpha-mannosidase is an enzyme with systematic name (1->2)-(1->6)-alpha-D-mannan D-mannohydrolase. This enzyme catalyses the following chemical reaction
Mannosylglycoprotein endo-beta-mannosidase is an enzyme. This enzyme catalyses the following chemical reaction:
References
- Athanasopoulos VI, Niranjan K, Rastall RA (2005). "The production, purification and characterisation of two novel alpha-D-mannosidases from Aspergillus phoenicis". Carbohydr. Res. 340 (4): 609–17. doi:10.1016/j.carres.2005.01.005. PMID 15721331.
