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Difference between revisions of "Glycoside Hydrolase Family 86"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | To date, all characterized [[glycoside hydrolases]] of family 86 are β-agarases (EC [{{EClink}}3.2.1.81 3.2.1.81]) that cleave β-1,4 glycosidic bonds of agarose, releasing neoagaro-biose -tetraose and -hexaose. To date three enzymes, AgrA from ''Pseudoalteromonas atlantica'', AgaO from ''Microbulbifer thermotolerans JAMB-A94'' and Aga86E from ''Saccharophagus degradans'' and have been reported to be pure exo-β-agarases <cite>REF1,REF2,REF3</cite>. | |
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| Line 53: | Line 51: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #REF1 pmid=2914859 |
| − | # | + | #REF2 pmid=15170112 |
| − | # | + | #REF3 pmid=16672483 |
| − | + | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH086]] | [[Category:Glycoside Hydrolase Families|GH086]] | ||
Revision as of 01:18, 19 November 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.
- 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, releasing neoagaro-biose -tetraose and -hexaose. To date three enzymes, AgrA from Pseudoalteromonas atlantica, AgaO from Microbulbifer thermotolerans JAMB-A94 and Aga86E from Saccharophagus degradans and have been reported to be pure exo-β-agarases [1, 2, 3].
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, Nogi Y, Miyazaki M, Li Z, Hatada Y, Ito S, and Horikoshi K. (2004). Enzymatic properties and nucleotide and amino acid sequences of a thermostable beta-agarase from the novel marine isolate, JAMB-A94. Biosci Biotechnol Biochem. 2004;68(5):1073-81. DOI:10.1271/bbb.68.1073 |
- 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 |