Glycoside Hydrolase Family 85

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• Author: ^^^Wade Abbott^^^
• Responsible Curator: ^^^Al Boraston^^^

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Glycoside Hydrolase Family GHnn
Clan	GH-x
Mechanism	retaining/inverting
Active site residues	known/not known
CAZy DB link
http://www.cazy.org/fam/GHnn.html

    Normal   0               false   false   false      EN-US   X-NONE   X-NONE                                                     MicrosoftInternetExplorer4

Substrate specificities

GH85 enzymes, commonly referred to as Endo-beta-N-acetylglucosaminidases (ENGse) cleave the chitobiose core (GlcNAc-beta-1,4-GlcNac) of N-linked glycans. Examples of ENGases have been shown to be active on high-mannose type N-glycans (Endo-H, Endo-A, Endo-Fsp, Endo-F1, and Endo-E), bi- and tri-antennary complex type N-glycans (Endo-F2 and Endo-F3), and both substrates (Endo-M). Although specificity appears to be primarily determined by the oligosaccharide glycone[1], there is evidence that structural features within the carbohydrate-protein aglycone region (GlcNAc-Asn) may also play a role in substrate recognition. GH85s are broadly distributed in nature having been described in bacteria [2, 3, 4, 5], fungi [6], plants [7] and animals [8]. In several cases, including Endo-A from Arthrobacter protophormiae (ApGH85) and Endo-M from Mucor hiemalis (MhGH85), ENGases have been shown to catalyze transglycosylation reactions, making them useful candidates in the bioengineering of glycoproteins [1] and biologic pharmaceuticals [9].

References

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[[Category:Glycoside Hydrolase Families|GHnnn]]