CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Glycoside Hydrolase Family 82"
| Line 36: | Line 36: | ||
== 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>. | + | To date, a crystal structure has only been determined for the iota-carrageenase from ''A. fortis'' <cite>2</cite>. The crystal structure of a product complex has shed light on the existance of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme <cite>3</cite>. |
| Line 42: | Line 42: | ||
;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 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: not determined yet. |
| − | ;First general base residue identification: | + | ;First general base residue identification: not determined yet. |
;First 3-D structure: | ;First 3-D structure: | ||
| − | iota-carrageenase from ''A. fortis'' <cite>2</cite>. The structure belongs to the β-helix fold | + | iota-carrageenase from ''A. fortis'' <cite>2</cite>. The structure belongs to the β-helix fold ([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 00:43, 8 January 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.
| 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]. The crystal structure of a product complex has shed light on the existance of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme [3].
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
- not determined yet.
- First general base residue identification
- not determined yet.
- First 3-D structure
iota-carrageenase from A. fortis [2]. The structure belongs to the β-helix fold (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 |