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Difference between revisions of "Glycoside Hydrolase Family 48"
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== References == | == References == | ||
<biblio> | <biblio> | ||
+ | |||
#Comfort2007 pmid=17323919 | #Comfort2007 pmid=17323919 | ||
#He1999 pmid=9312086 | #He1999 pmid=9312086 | ||
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#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | ||
+ | #Wang1993 pmid=8444792 | ||
+ | #Guimaraes2002 pmid=12096911 | ||
+ | #Parsiegla1998 pmid=9755156 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH048]] | [[Category:Glycoside Hydrolase Families|GH048]] |
Revision as of 04:08, 14 February 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.
- Author: ^^^Bareket Dassa^^^
- Responsible Curator: ^^^Ed Bayer^^^
Glycoside Hydrolase Family GH48 | |
Clan | GH-M |
Mechanism | inverting |
Active site residues | not known |
CAZy DB link | |
http://www.cazy.org/fam/GH48.html |
Substrate specificities
Content is to be added here.
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
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 sterochemistry 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 [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
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 |
- 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 |
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- Wang WK, Kruus K, and Wu JH. (1993). Cloning and DNA sequence of the gene coding for Clostridium thermocellum cellulase Ss (CelS), a major cellulosome component. J Bacteriol. 1993;175(5):1293-302. DOI:10.1128/jb.175.5.1293-1302.1993 |
- Guimarães BG, Souchon H, Lytle BL, David Wu JH, and Alzari PM. (2002). The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome. J Mol Biol. 2002;320(3):587-96. DOI:10.1016/s0022-2836(02)00497-7 |
- Parsiegla G, Juy M, Reverbel-Leroy C, Tardif C, Belaïch JP, Driguez H, and Haser R. (1998). The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A resolution. EMBO J. 1998;17(19):5551-62. DOI:10.1093/emboj/17.19.5551 |