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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5. Abbott DW, Ficko-Blean E, van Bueren AL, Rogowski A, Cartmell A, Coutinho PM, Henrissat B, Gilbert HJ, and Boraston AB. (2009). Analysis of the structural and functional diversity of plant cell wall specific family 6 carbohydrate binding modules. Biochemistry. 2009;48(43):10395-404. DOI:10.1021/bi9013424 |

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[[Category:Glycoside Hydrolase Families|GHnnn]]