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 See a page that's out-of-date and just needs a touch-up?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.
Glycoside Hydrolase Family 86
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: ^^^Mirjam Czjzek^^^
- Responsible Curator: ^^^Mirjam Czjzek^^^
| Glycoside Hydrolase Family GH86 | |
| Clan | GH-A |
| Mechanism | probably retaining |
| Active site residues | inferred from clan GH-A as two Glu |
| CAZy DB link | |
| https://www.cazy.org/GH86.html | |
Substrate specificities
To date, all characterized glycoside hydrolases of family 86 are β-agarases (EC 3.2.1.81) that cleave β-1,4 glycosidic bonds of agarose. To date three enzymes have been characterized: AgrA from Pseudoalteromonas atlantica, AgaO from Microbulbifer thermotolerans JAMB-A94 and Aga86E from Saccharophagus degradans 2-40 [1, 2, 3]. AgaO from M. thermotolerans was reported to be an endo-hydrolytic enzyme, releasing neoagaro-hexaose as main product [2], while the recombinant Aga86E from S. degradans released only neoagarobiose in an exo-acting manner.
Kinetics and Mechanism
Actually, a potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan GH-A enzymes https://www.cazy.org/GH86.html. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.
Catalytic Residues
Actually, the catalytic residues can only be inferred from analogy to clan GH-A enzymes as two glutamate residues.
Three-dimensional structures
No 3D structure is available to date.
Family Firsts
- First stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [5].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [6].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [7].
References
- Belas R (1989). Sequence analysis of the agrA gene encoding beta-agarase from Pseudomonas atlantica. J Bacteriol. 1989;171(1):602-5. DOI:10.1128/jb.171.1.602-605.1989 |
- Ohta Y, Hatada Y, Nogi Y, Li Z, Ito S, and Horikoshi K. (2004). Cloning, expression, and characterization of a glycoside hydrolase family 86 beta-agarase from a deep-sea Microbulbifer-like isolate. Appl Microbiol Biotechnol. 2004;66(3):266-75. DOI:10.1007/s00253-004-1757-5 |
- Ekborg NA, Taylor LE, Longmire AG, Henrissat B, Weiner RM, and Hutcheson SW. (2006). Genomic and proteomic analyses of the agarolytic system expressed by Saccharophagus degradans 2-40. Appl Environ Microbiol. 2006;72(5):3396-405. DOI:10.1128/AEM.72.5.3396-3405.2006 |