Glycoside hydrolase family 38
Encyclopedia
In molecular biology, glycoside hydrolase family 38 is a family
of glycoside hydrolases
.
Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond
between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 38 CAZY GH_38 comprises enzymes with only one known activity; alpha-mannosidase
.
Lysosomal alpha-mannosidase is necessary for the catabolism
of N-linked carbohydrates released during glycoprotein
turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose
residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis
(AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.
A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.
Protein family
A protein family is a group of evolutionarily-related proteins, and is often nearly synonymous with gene family. The term protein family should not be confused with family as it is used in taxonomy....
of glycoside hydrolases
Glycoside hydrolase
Glycoside hydrolases catalyze the hydrolysis of the glycosidic linkage to release smaller sugars...
.
Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond
Glycosidic bond
In chemistry, a glycosidic bond is a type of covalent bond that joins a carbohydrate molecule to another group, which may or may not be another carbohydrate....
between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 38 CAZY GH_38 comprises enzymes with only one known activity; alpha-mannosidase
Alpha-Mannosidase
alpha-Mannosidase is an enzyme involved in the cleavage of the alpha form of mannose.- Isozymes :Humans express the following three alpha-mannosidase isozymes:- Applications :...
.
Lysosomal alpha-mannosidase is necessary for the catabolism
Catabolism
Catabolism is the set of metabolic pathways that break down molecules into smaller units and release energy. In catabolism, large molecules such as polysaccharides, lipids, nucleic acids and proteins are broken down into smaller units such as monosaccharides, fatty acids, nucleotides, and amino...
of N-linked carbohydrates released during glycoprotein
Glycoprotein
Glycoproteins are proteins that contain oligosaccharide chains covalently attached to polypeptide side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. In proteins that have segments extending...
turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose
Mannose
Mannose is a sugar monomer of the aldohexose series of carbohydrates. Mannose is a C-2 epimer of glucose. It is not part of human metabolism, but is a component of microbial cell walls, and is therefore a target of the immune system and also of antibiotics....
residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis
Alpha-mannosidosis
Alpha-mannosidosis is a lysosomal storage disorder caused by deficient activity of the enzyme alpha-D-mannosidase . In humans it is known to be caused by an autosomal recessive genetic mutation...
(AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.
A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.