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Difference between revisions of "Glycoside Hydrolase Family 35"
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Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini. | Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini. | ||
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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<biblio> | <biblio> | ||
#Tanthanuch2008 pmid=18664295 | #Tanthanuch2008 pmid=18664295 | ||
+ | #Kawarabayasi1998 pmid=96794 | ||
+ | #Fukui2005 pmid=15710748 | ||
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#Comfort2007 pmid=17323919 | #Comfort2007 pmid=17323919 | ||
#He1999 pmid=9312086 | #He1999 pmid=9312086 |
Revision as of 03:12, 4 October 2010
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Authors: ^^^Alexander Golubev^^^ and ^^^Anna Kulminskaya^^^
- Responsible Curator: ^^^Anna Kulminskaya^^^
Glycoside Hydrolase Family GH35 | |
Clan | GH-A |
Mechanism | retaining (inferred) |
Active site residues | known |
CAZy DB link | |
https://www.cazy.org/GH35.html |
Substrate specificities
The major activity of enzymes of this GH family is β-galactosidase (EC 3.2.1.23). Enzymes were isolated from microorganisms such as fungi, bacteria and yeasts; plants, animals cells, and from recombinant sources. The β-galactosidase (EC 3.2.1.23) catalyses the hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides as, for example, lactose (1,4-O-β-D-galactopyranosyl-D-glucose) and structurally related compounds. GH35 includes multiple genes in various plant species [1], suggesting ubiquity of GH35 gene multiplicity in plants. The enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production of galactosylated products.
Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.
Kinetics and Mechanism
Content is to be added here.
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 [1].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [3].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [4].
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 enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 |
- Tanthanuch W, Chantarangsee M, Maneesan J, and Ketudat-Cairns J. (2008). Genomic and expression analysis of glycosyl hydrolase family 35 genes from rice (Oryza sativa L.). BMC Plant Biol. 2008;8:84. DOI:10.1186/1471-2229-8-84 |
- Davis E (1978). Vaccine damaged children. Australas Nurses J. 1978;7(8):3-6. | Google Books | Open Library
- Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S, and Imanaka T. (2005). Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 2005;15(3):352-63. DOI:10.1101/gr.3003105 |