Protein Domain : Glycosyl hydrolases family 18 (GH18) active site IPR001579

Type  Active_site
Description  The glycosyl hydrolases family 18 (GH18) is widely distributed in all domains of life. The GH18 family contains hydrolytic enzymes with chitinase or endo-N-acetyl-beta-D-glucosaminidase (ENGase) activity as well as chitinase like lectins (chi-lectins/proteins (CLPs). Chitinases (EC 3.2.1.14) are hydrolytic enzymes that cleave the beta-1,4-bond releasing oligomeric, dimeric (chitobiose) or monomeric (N-actetylglucosamine, GlcNAc) products. ENGases (EC ) hydrolyse the beta-1,4 linkage in the chitobiose core of N-linked glycans from glycoproteins leaving one GlcNAc residue on the substrate. CLPs do not display chitinase activity but some of them have been reported to have specific functions and carbohydrate binding property. The catalytic domain of GH18s may be connected to one or several substrate binding modules (CBMs), which enhance binding of enzymes to insoluble substrates. Certain GH18s also contain peptide signals for localization such as an N-terminal secretion peptide, a C-terminal glycosyl-phosphatidylinositol (GPI) anchor signal for attachment to the plasma-membrane, or N- or O-linked glycosylation sites for oligosaccharide modifications [ , , , , , , , , ].The catalytic domain of GH18s has a common (beta/alpha)8 triosephosphate isomerase (TIM)-barrel structure, which consists of a barrel-like framework made from eight internal parallel β-strands that are alternately connected by eight exterior α-helices. The active site motif DxxDxDxE is essential for the activity of the GH18 catalytic domain. The Glu (E) in this motif acts as the catalytic proton donor, and the last Asp (D(3))is supposed to contribute to the stabilization of the essential distortion of the substrate [ , , , , ].This entry represents the active site of GH18 members predominantly found in bacteria and eukaryota.
Short Name  Glyco_hydro_18_chit_AS

0 Child Features

0 Gene Families

1000 Genes

2 Ontology Annotations

0 Parent Features

13 Publications

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