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Glycoside Hydrolase Family 63
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- Author: ^^^Takashi Tonozuka^^^
- Responsible Curator: ^^^Takashi Tonozuka^^^
| Glycoside Hydrolase Family GH63 | |
| Clan | GH-G |
| Mechanism | inverting |
| Active site residues | Inferred |
| CAZy DB link | |
| https://www.cazy.org/GH63.html | |
Substrate specificities
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the N-linked oligosacharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α-glucosidase I from Saccharomyces cerevisiae, have been most intensively studied.
Genes for the GH63 enzymes have also been found in archaea and bacteria, but archaea and bacteria have been reported not to produce eukaryotic N-linked oligosacharides, and the principal substrates of archaeal and bacterial GH63 enzymes are still unclear. A bacterial GH63 enzyme, Escherichia coli YgjK, showed the highest activity for the α-1,3-glucosidic linkage of nigerose among commercially available sugars [1].
Kinetics and Mechanism
Family GH63 enzymes are inverting enzymes, as first shown by NMR on a processing α-glucosidase I from Saccharomyces cerevisiae [2].
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 [2].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [1].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [1].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [1].
References
- Kurakata Y, Uechi A, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, and Tonozuka T. (2008). Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63. J Mol Biol. 2008;381(1):116-28. DOI:10.1016/j.jmb.2008.05.061 |
- Palcic MM, Scaman CH, Otter A, Szpacenko A, Romaniouk A, Li YX, and Vijay IK. (1999). Processing alpha-glucosidase I is an inverting glycosidase. Glycoconj J. 1999;16(7):351-5. DOI:10.1023/a:1007096011392 |