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Glycoside Hydrolase Family 75
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- Author:
- Responsible Curator: ^^^Ryszard Brzezinski^^^
| Glycoside Hydrolase Family GH75 | |
| Clan | Not assigned |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH75.html | |
Substrate specificities
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity [1, 2]. The analysis of the final product of hydrolysis of partially N-deacetylated chitosan by the GH75 chitosanase from Aspergillus fumigatus suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain [3].
Kinetics and Mechanism
Family GH46 enzymes utilize an inverting mechanism as shown by NMR [3].
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [5].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [6].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [7].
References
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Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, Fusarium solani f.sp. phaseoli - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.
- Cheng CY and Li YK. (2000). An Aspergillus chitosanase with potential for large-scale preparation of chitosan oligosaccharides. Biotechnol Appl Biochem. 2000;32(3):197-203. DOI:10.1042/ba20000063 |
- Cheng CY, Chang CH, Wu YJ, and Li YK. (2006). Exploration of glycosyl hydrolase family 75, a chitosanase from Aspergillus fumigatus. J Biol Chem. 2006;281(6):3137-44. DOI:10.1074/jbc.M512506200 |