Glycoside hydrolase family 65
| Glycosyl hydrolase family 65, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 maltose phosphorylase from lactobacillus brevis | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_65N | ||||||||
| Pfam | PF03636 | ||||||||
| Pfam clan | CL0103 | ||||||||
| InterPro | IPR005196 | ||||||||
| SCOP2 | 1h54 / SCOPe / SUPFAM | ||||||||
| CAZy | GH65 | ||||||||
| |||||||||
| Glycosyl hydrolase family 65 central catalytic domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
maltose phosphorylase from lactobacillus brevis | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_65m | ||||||||
| Pfam | PF03632 | ||||||||
| Pfam clan | CL0059 | ||||||||
| InterPro | IPR005195 | ||||||||
| SCOP2 | 1h54 / SCOPe / SUPFAM | ||||||||
| CAZy | GH65 | ||||||||
| |||||||||
| Glycosyl hydrolase family 65, C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
maltose phosphorylase from lactobacillus brevis | |||||||||
| Identifiers | |||||||||
| Symbol | Glyco_hydro_65C | ||||||||
| Pfam | PF03633 | ||||||||
| InterPro | IPR005194 | ||||||||
| SCOP2 | 1h54 / SCOPe / SUPFAM | ||||||||
| CAZy | GH65 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 65 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. 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.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
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.[6] 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.[6] The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity[6] although its precise function remains unknown.
References
- ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ^ a b c van Tilbeurgh H, Egloff MP, Uppenberg J, Haalck L (2001). "Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases". Structure. 9 (8): 689–697. doi:10.1016/S0969-2126(01)00626-8. PMID 11587643.
{{cite journal}}: CS1 maint: multiple names: authors list (link)