PF00704

Glycosyl hydrolases family 18

Pfam entry
Member databasePfam
Pfam typedomain
Short nameGlyco_hydro_18
ClanTIM_barrel
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description
Imported from IPR001223

The glycosyl hydrolases family 18 (GH18)
GH18
is widely distributed in all kingdoms and 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 (
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 (
3.2.1.96
) hydrolyze 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
[3]
. This family also includes glycoproteins from mammals, such as oviduct-specific glycoproteins.

This entry represents the catalytic domain of GH18s, which has a common (β/α)8 triosephosphate isomerase (TIM)-barrel structure that 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.
[6, 5, 4]
.

O-Glycosyl hydrolases (
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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families
[2, 1]
. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.

References
Imported from IPR001223

1.Structures and mechanisms of glycosyl hydrolases. Davies G, Henrissat B. Structure 3, 853-9, (1995). View articlePMID: 8535779

2.Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Proc. Natl. Acad. Sci. U.S.A. 92, 7090-4, (1995). View articlePMID: 7624375

3.Chitinase-like proteins in lung injury, repair, and metastasis. Lee CG, Dela Cruz CS, Ma B, Ahangari F, Zhou Y, Halaban R, Sznol M, Elias JA. Proc Am Thorac Soc 9, 57-61, (2012). View articlePMID: 22550243

4.Structure of chitinase D from Serratia proteamaculans reveals the structural basis of its dual action of hydrolysis and transglycosylation. Madhuprakash J, Singh A, Kumar S, Sinha M, Kaur P, Sharma S, Podile AR, Singh TP. Int J Biochem Mol Biol 4, 166-78, (2013). PMID: 24380021

5.High resolution crystal structure of the endo-N-Acetyl-β-D-glucosaminidase responsible for the deglycosylation of Hypocrea jecorina cellulases. Stals I, Karkehabadi S, Kim S, Ward M, Van Landschoot A, Devreese B, Sandgren M. PLoS ONE 7, e40854, (2012). PMID: 22859955

6.Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties. Schimpl M, Rush CL, Betou M, Eggleston IM, Recklies AD, van Aalten DM. Biochem. J. 446, 149-57, (2012). View articlePMID: 22742450

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