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Difference between revisions of "Glycoside Hydrolase Family 36"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | Family GH36 alpha-galactosidases are anomeric configuration-retaining enzymes | + | Family GH36 alpha-galactosidases are anomeric configuration-retaining enzymes, as first shown by NMR studies on the alpha-galactosidase GalA from ''Thermotoga maritima'' <cite>1</cite>. Correspondingly, GH36 enzymes use a classical Koshland double-displacement mechanism <cite>4</cite>, like their [[Glycoside Hydrolase Family GH27 (GH27)]] relatives in Clan GH-D. |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 12:18, 27 May 2007
| Glycoside Hydrolase Family GH36 | |
| Clan | GH-D |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH36.html | |
Substrate specificities
Alpha-galactosidase and alpha-N-acetylgalactosaminidase activity has been demonstrated in archaeal, bacterial, and eukaryotic members of this family. Additionally, certain plant members of this family possess stachyose synthase or raffinose synthase activity.
Kinetics and Mechanism
Family GH36 alpha-galactosidases are anomeric configuration-retaining enzymes, as first shown by NMR studies on the alpha-galactosidase GalA from Thermotoga maritima [1]. Correspondingly, GH36 enzymes use a classical Koshland double-displacement mechanism [2], like their Glycoside Hydrolase Family GH27 (GH27) relatives in Clan GH-D.
Catalytic Residues
Three-dimensional structures
Family Firsts
- First sterochemistry determination
- Thermotoga maritima alpha-galactosidase, by NMR [1].
- First catalytic nucleophile identification
- Sulfolobus solfataricus alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis [3]. Subsequently confirmed in Thermotoga maritima alpha-galactosidase by structural homology, mutagenesis, and azide rescue [1].
- First general acid/base residue identification
- Sulfolobus solfataricus alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis [3]. Subsequently confirmed in Thermotoga maritima alpha-galactosidase by structural homology, mutagenesis, and azide rescue [1].
- First 3-D structure
- Thermotoga maritima alpha-galactosidase. Coordinates first reported as part of a high-throughput functional genomics project [4], structural analysis reported in ref. [1].
References
- Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- Brouns SJ, Smits N, Wu H, Snijders AP, Wright PC, de Vos WM, and van der Oost J. (2006). Identification of a novel alpha-galactosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. J Bacteriol. 2006;188(7):2392-9. DOI:10.1128/JB.188.7.2392-2399.2006 |
- Lesley SA, Kuhn P, Godzik A, Deacon AM, Mathews I, Kreusch A, Spraggon G, Klock HE, McMullan D, Shin T, Vincent J, Robb A, Brinen LS, Miller MD, McPhillips TM, Miller MA, Scheibe D, Canaves JM, Guda C, Jaroszewski L, Selby TL, Elsliger MA, Wooley J, Taylor SS, Hodgson KO, Wilson IA, Schultz PG, and Stevens RC. (2002). Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc Natl Acad Sci U S A. 2002;99(18):11664-9. DOI:10.1073/pnas.142413399 |