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Difference between revisions of "Glycoside Hydrolase Family 82"
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== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | From structural analysis predicted to be two out of the three candidate amino acids Glu245, Asp247 or Glu310 <cite>2</cite>. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | To date a crystal structure has only been determined for the iota-carrageenase from ''A. fortis'' <cite>2</cite>. | |
== Family Firsts == | == Family Firsts == | ||
| + | ;First sequence identification and family creation: iota-carrageenase sequences have been first reported for enzymes from ''A. fortis'' and ''Z. galactanivorans'' <cite>1</cite>. | ||
;First sterochemistry determination: GH82 enzymes are inverting as shown by NMR <cite>1</cite>. | ;First sterochemistry determination: GH82 enzymes are inverting as shown by NMR <cite>1</cite>. | ||
;First general acid residue identification: | ;First general acid residue identification: | ||
;First general base residue identification: | ;First general base residue identification: | ||
;First 3-D structure: | ;First 3-D structure: | ||
| − | iota-carrageenase from '' | + | iota-carrageenase from ''A. fortis'' <cite>2</cite>. The structure belongs to the β-helix fold (PDB ID [{{PDBlink}}1h80 1h80])([http://www.rcsb.org/pdb/explore/explore.do?structureId=1H80 PDB 1h80] and [http://www.rcsb.org/pdb/explore/explore.do?structureId=1KTW PDB 1ktw]). |
== References == | == References == | ||
Revision as of 00:17, 8 January 2010
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| Glycoside Hydrolase Family GH82 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH82.html | |
Substrate specificities
The two known members of glycoside hydrolase family 82 enzymes cleave the β-1,4 galactosidic bond of the marine algal polysaccharide iota-carrageenan [1] yielding products of the neocarrabiose series.
Kinetics and Mechanism
Family 82 enzymes are inverting enzymes, as first shown by NMR [1] on the iota-carrageenase from Alteromonas fortis.
Catalytic Residues
From structural analysis predicted to be two out of the three candidate amino acids Glu245, Asp247 or Glu310 [2].
Three-dimensional structures
To date a crystal structure has only been determined for the iota-carrageenase from A. fortis [2].
Family Firsts
- First sequence identification and family creation
- iota-carrageenase sequences have been first reported for enzymes from A. fortis and Z. galactanivorans [1].
- First sterochemistry determination
- GH82 enzymes are inverting as shown by NMR [1].
- First general acid residue identification
- First general base residue identification
- First 3-D structure
iota-carrageenase from A. fortis [2]. The structure belongs to the β-helix fold (PDB ID 1h80)(PDB 1h80 and PDB 1ktw).
References
- Barbeyron T, Michel G, Potin P, Henrissat B, and Kloareg B. (2000). iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases. J Biol Chem. 2000;275(45):35499-505. DOI:10.1074/jbc.M003404200 |
- Michel G, Chantalat L, Fanchon E, Henrissat B, Kloareg B, and Dideberg O. (2001). The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J Biol Chem. 2001;276(43):40202-9. DOI:10.1074/jbc.M100670200 |
- Michel G, Helbert W, Kahn R, Dideberg O, and Kloareg B. (2003). The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae. J Mol Biol. 2003;334(3):421-33. DOI:10.1016/j.jmb.2003.09.056 |