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Difference between revisions of "Glycoside Hydrolase Family 78"
Zui Fujimoto (talk | contribs) |
Zui Fujimoto (talk | contribs) |
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|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | | | + | |GH-M |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
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|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 32: | Line 32: | ||
== 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 | + | GH78 enzymes hydrolyze glycosidic bonds through an acid base-assisted single displacement or inverting mechanism elucidated by proton NMR <cite>Zverlov2000</cite>.. |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 41: | Line 41: | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: ''Clostridium stercorarium'' α-L-rhamnosidase RamA by <sup>1</sup>H-NMR. | + | ;First stereochemistry determination: ''Clostridium stercorarium'' α-L-rhamnosidase RamA, by <sup>1</sup>H-NMR <cite>Zverlov2000</cite>. |
| − | ;First | + | ;First general base residue identification: ''Streptomyces avermitilis'' α-L-rhamnosidase (SaRha78A), based on mutagensis informed by 3D structural data <cite>Fujimoto2013</cite>. |
| − | ;First general acid | + | ;First general acid residue identification: ''Streptomyces avermitilis'' α-L-rhamnosidase (SaRha78A), based on mutagensis informed by 3D structural data <cite>Fujimoto2013</cite>. |
| − | ;First 3-D structure: α-L-rhamnosidase B (BsRhaB) | + | ;First 3-D structure: ''Bacillus'' sp. GL1 α-L-rhamnosidase B (BsRhaB) <cite>Cui2007</cite>. |
== References == | == References == | ||
| Line 52: | Line 52: | ||
#Zverlov2000 pmid=10632887 | #Zverlov2000 pmid=10632887 | ||
#Cui2007 pmid=17936784 | #Cui2007 pmid=17936784 | ||
| + | #Fujimoto2013 pmid=23486481 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH078]] | [[Category:Glycoside Hydrolase Families|GH078]] | ||
Revision as of 19:01, 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 | GH-M |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| https://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 [1]..
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 [1].
- First general base residue identification
- Streptomyces avermitilis α-L-rhamnosidase (SaRha78A), based on mutagensis informed by 3D structural data [2].
- First general acid residue identification
- Streptomyces avermitilis α-L-rhamnosidase (SaRha78A), based on mutagensis informed by 3D structural data [2].
- First 3-D structure
- Bacillus sp. GL1 α-L-rhamnosidase B (BsRhaB) [3].
References
- Zverlov VV, Hertel C, Bronnenmeier K, Hroch A, Kellermann J, and Schwarz WH. (2000). The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase. Mol Microbiol. 2000;35(1):173-9. DOI:10.1046/j.1365-2958.2000.01691.x |
- Fujimoto Z, Jackson A, Michikawa M, Maehara T, Momma M, Henrissat B, Gilbert HJ, and Kaneko S. (2013). The structure of a Streptomyces avermitilis α-L-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement. J Biol Chem. 2013;288(17):12376-85. DOI:10.1074/jbc.M113.460097 |
- Cui Z, Maruyama Y, Mikami B, Hashimoto W, and Murata K. (2007). Crystal structure of glycoside hydrolase family 78 alpha-L-Rhamnosidase from Bacillus sp. GL1. J Mol Biol. 2007;374(2):384-98. DOI:10.1016/j.jmb.2007.09.003 |
- 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 |
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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