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Glycoside Hydrolase Family 135
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- Author: ^^^Spencer Williams^^^
- Responsible Curator: ^^^Spencer Williams^^^
| Glycoside Hydrolase Family GH135 | |
| Clan | none |
| Mechanism | unknown |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH135.html | |
Substrate specificities
A single report has disclosed fungal glycoside hydrolases with the ability to degrade a fungal heteropolysaccharide galactosaminogalactan (GAG) [1]. GAG is produced by Aspergillus fumigatus as an exopolysaccharide, which is α-1,4- linked galactose, N-acetylgalactosamine, and galactosamine residues, and which is found in both a secreted form and bound to the cell wall of hyphae. The recombinant protein purified and cell wall-associated GAG. While it is unclear precisely where within the GAG chain the enzyme acts, and thus whether it should be considered an α-galactosidase, α-galactosaminase or an α-galactosaminidase, and 3-D complex of the protein with N-acetylgalactosamine (see below) is suggestive that the enzyme possesses α-galactosaminidase activity.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Three-dimensional structures are available for one GH family 135 member, Aspergillus clavatus Sph3 [1]. This protein has a classical (β/α)8 TIM barrel fold.with similarities to glycoside hydrolase families 18,
27, and 84
Family Firsts
- First stereochemistry determination
- Unknown.
- First catalytic nucleophile identification
- Unknown.
- First general acid/base residue identification
- Unknown.
- First 3-D structure
- Sph3 from Aspergillus clavatus [1].
References
- Bamford NC, Snarr BD, Gravelat FN, Little DJ, Lee MJ, Zacharias CA, Chabot JC, Geller AM, Baptista SD, Baker P, Robinson H, Howell PL, and Sheppard DC. (2015). Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus. J Biol Chem. 2015;290(46):27438-50. DOI:10.1074/jbc.M115.679050 |