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Difference between revisions of "Glycoside Hydrolase Family 78"
Harry Brumer (talk | contribs) (Zui Fujimoto new Responsible Curator) |
Zui Fujimoto (talk | contribs) |
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{| {{Prettytable}} | {| {{Prettytable}} | ||
|- | |- | ||
| − | |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family | + | |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH78''' |
|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | | | + | | |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |inverting |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| Line 22: | Line 22: | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
|- | |- | ||
| − | | colspan="2" |{{CAZyDBlink}} | + | | colspan="2" |{{CAZyDBlink}}GH78.html |
|} | |} | ||
</div> | </div> | ||
| Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | + | Family GH78 glycoside hydrolases are found in bacteria and fungi. The characterized activity of this family is α-L-rhamnosidase (EC 3.2.1.40). α-L-Rhamnosidases catalyze the hydrolysis of α-L-rhamnosyl-linkages in L-rhamnose containing compounds, such as naringin and rutin, or rhamnogalacturonan and arabinogalactan-protein. | |
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | GH78 enzymes hydrolyze glycosidic bonds through an acid base-assisted single displacement or inverting mechanism elucidated by proton NMR [Zverlov2000]. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 43: | Line 41: | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: ''Clostridium stercorarium'' α-L-rhamnosidase RamA by <sup>1</sup>H-NMR. |
;First catalytic nucleophile identification: Content is to be added here. | ;First catalytic nucleophile identification: Content is to be added here. | ||
;First general acid/base residue identification: Content is to be added here. | ;First general acid/base residue identification: Content is to be added here. | ||
| − | ;First 3-D structure: | + | ;First 3-D structure: α-L-rhamnosidase B (BsRhaB) from ''Bacillus'' sp. GL1 [Cui2007]. |
== References == | == References == | ||
| Line 53: | Line 51: | ||
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382] | #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382] | ||
</biblio> | </biblio> | ||
| − | + | #Zverlov2000 pmid=10632887 | |
| + | #Cui2007 pmid=17936784 | ||
[[Category:Glycoside Hydrolase Families|GH078]] | [[Category:Glycoside Hydrolase Families|GH078]] | ||
Revision as of 19:10, 19 May 2014
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:
- Responsible Curator: ^^^Zui Fujimoto^^^
| Glycoside Hydrolase Family GH78 | |
| Clan | |
| Mechanism | inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| http://www.cazy.org/GH78.html | |
Substrate specificities
Family GH78 glycoside hydrolases are found in bacteria and fungi. The characterized activity of this family is α-L-rhamnosidase (EC 3.2.1.40). α-L-Rhamnosidases catalyze the hydrolysis of α-L-rhamnosyl-linkages in L-rhamnose containing compounds, such as naringin and rutin, or rhamnogalacturonan and arabinogalactan-protein.
Kinetics and Mechanism
GH78 enzymes hydrolyze glycosidic bonds through an acid base-assisted single displacement or inverting mechanism elucidated by proton NMR [Zverlov2000].
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Clostridium stercorarium α-L-rhamnosidase RamA by 1H-NMR.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- α-L-rhamnosidase B (BsRhaB) from Bacillus sp. GL1 [Cui2007].
References
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
-
Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382
- Zverlov2000 pmid=10632887
- Cui2007 pmid=17936784