Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.

Domain of unknown function (DUF1735). This domain of unknown function is found in a number of bacterial proteins including acylhydrolases. The structure of this domain has a beta-sandwich fold.

The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.

Crystalstructure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],6T8K_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8K_B Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8L_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man9GlcNAc product in P212121 [Bacteroides thetaiotaomicron VPI-5482],6TCW_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man5GlcNAc product [Bacteroides thetaiotaomicron VPI-5482],7NWF_A Chain A, Endo-beta-N-acetylglucosaminidase F1 [Bacteroides thetaiotaomicron VPI-5482]

Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482]

Crystalstructure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.55 A resolution [Bacteroides thetaiotaomicron VPI-5482]

CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica]

ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]

Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1

Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1

Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2