Glycoside hydrolase family 65
Encyclopedia
In molecular biology, glycoside hydrolase family 65 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.
This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase
and maltose phosphorylases
. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose
and inorganic phosphate into beta-D-glucose-1-phosphate and glucose
.
It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity although its precise function remains unknown.
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.
This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase
Trehalase
Trehalase is a glycoside hydrolase enzyme that catalyzes the conversion of trehalose to glucose. It is found in most animals.The non-reducing disaccharide trehalose is one of the most important storage carbohydrates, which is present in almost all forms of life except mammals...
and maltose phosphorylases
Maltose phosphorylase
In enzymology, a maltose phosphorylase is an enzyme that catalyzes the chemical reactionThus, the two substrates of this enzyme are maltose and phosphate, whereas its two products are D-glucose and beta-D-glucose 1-phosphate....
. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose
Maltose
Maltose , or malt sugar, is a disaccharide formed from two units of glucose joined with an αbond, formed from a condensation reaction. The isomer "isomaltose" has two glucose molecules linked through an α bond. Maltose is the second member of an important biochemical series of glucose chains....
and inorganic phosphate into beta-D-glucose-1-phosphate and glucose
Glucose
Glucose is a simple sugar and an important carbohydrate in biology. Cells use it as the primary source of energy and a metabolic intermediate...
.
It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity although its precise function remains unknown.