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Difference between revisions of "Glycoside Hydrolase Family 27"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | Alpha-galactosidase activity has been observed in both bacterial and eukaryotic members of GH27, while alpha-''N''-acetylgalactosaminidase acitivity has been observed in certain eukaryotic enzymes, including human, mouse, and chicken. Bacterial GH27 isomaltodextranases are also known. Notably, this family contains both human alpha-galactosidase A and human alpha-''N''-acetylgalactosaminidase (also known as alpha-galactosidase B), defects in which produce the phenotypes associated with Schindler and Fabry diseases, respectively <cite>4 5</cite>. | |
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#1 pmid=10085226 | #1 pmid=10085226 | ||
#2 pmid=10933800 | #2 pmid=10933800 | ||
| − | + | #3 pmid=12005440 | |
| + | #4 Garman, S.C. (2006) Structural studies on alpha-GAL and alpha-NAGAL: The atomic basis of Fabry and Schindler diseases. Biocatalysis and Biotransformation 24, 129-136. | ||
| + | #5 pmid=17391432 | ||
</biblio> | </biblio> | ||
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[[Category:Glycoside Hydrolase Families]] | [[Category:Glycoside Hydrolase Families]] | ||
Revision as of 15:21, 3 July 2007
| Glycoside Hydrolase Family GH27 | |
| Clan | GH-D |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH27.html | |
Substrate specificities
Alpha-galactosidase activity has been observed in both bacterial and eukaryotic members of GH27, while alpha-N-acetylgalactosaminidase acitivity has been observed in certain eukaryotic enzymes, including human, mouse, and chicken. Bacterial GH27 isomaltodextranases are also known. Notably, this family contains both human alpha-galactosidase A and human alpha-N-acetylgalactosaminidase (also known as alpha-galactosidase B), defects in which produce the phenotypes associated with Schindler and Fabry diseases, respectively [1, 2].
Kinetics and Mechanism
Catalytic Residues
Three-dimensional structures
Family Firsts
- First sterochemistry determination
- Retention of anomeric stereochemistry demonstrated by H-1 NMR for the main alpha-galactosidase from the white-rot fungus Phanerochaete chrysosporium [3].
- First catalytic nucleophile identification
- Phanerochaete chrysosporium alpha-galactosidase by mechanism-based labelling with 2',4',6'-trinitrophenyl 2-deoxy-2,2-difluoro-alpha-D-lyxo-hexopyranoside ("2,2-difluoro-alpha-galactosyl picrate"), pepsin digestion, and mass spectrometry [4].
- First general acid/base residue identification
- Chicken (Gallus gallus) N-acetylgalactosaminidase by X-ray structural analysis of an enzyme-N-acetylgalactosamine complex [5].
- First 3-D structure
- Chicken N-acetylgalactosaminidase, both free enzyme and in complex with N-acetylgalactosamine [5].
References
-
Garman, S.C. (2006) Structural studies on alpha-GAL and alpha-NAGAL: The atomic basis of Fabry and Schindler diseases. Biocatalysis and Biotransformation 24, 129-136.
- Garman SC (2007). Structure-function relationships in alpha-galactosidase A. Acta Paediatr. 2007;96(455):6-16. DOI:10.1111/j.1651-2227.2007.00198.x |
- Brumer H 3rd, Sims PF, and Sinnott ML. (1999). Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main alpha-galactosidase. Biochem J. 1999;339 ( Pt 1)(Pt 1):43-53. | Google Books | Open Library
- Hart DO, He S, Chany CJ 2nd, Withers SG, Sims PF, Sinnott ML, and Brumer H 3rd. (2000). Identification of Asp-130 as the catalytic nucleophile in the main alpha-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase. Biochemistry. 2000;39(32):9826-36. DOI:10.1021/bi0008074 |
- Garman SC, Hannick L, Zhu A, and Garboczi DN. (2002). The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. Structure. 2002;10(3):425-34. DOI:10.1016/s0969-2126(02)00726-8 |