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Difference between revisions of "Glycoside Hydrolase Family 86"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | [[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. As of November 2010, only three enzymes have been characterized: AgrA from ''Pseudoalteromonas atlantica'', AgaO from ''Microbulbifer thermotolerans JAMB-A94'' and Aga86E from ''Saccharophagus degradans 2-40'' <cite>Belas1989,Ohta2004,Ekborg2006</cite>. AgaO from ''M. thermotolerans'' was reported to be an endo-hydrolytic enzyme, releasing neoagaro-hexaose as main product <cite>Ohta2004</cite>, while the recombinant Aga86E from ''S. degradans'' released only neoagarobiose in an exo-acting manner <cite>Ekborg2006</cite>. | |
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | A potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan [{{CAZyDBlink}}Glycoside-Hydrolases.html GH-A enzymes]. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date. | |
| − | |||
== Catalytic Residues == | == Catalytic Residues == | ||
Actually, the catalytic residues can only be inferred from analogy to clan GH-A enzymes as two glutamate residues. | Actually, the catalytic residues can only be inferred from analogy to clan GH-A enzymes as two glutamate residues. | ||
| − | |||
== Three-dimensional structures == | == Three-dimensional structures == | ||
No 3D structure is available to date. | No 3D structure is available to date. | ||
| − | |||
== Family Firsts == | == Family Firsts == | ||
| − | ;Identification of first family member: The first member of this family, AgrA, was identified in ''Pseudoalteromonas atlantica'' <cite> | + | ;Identification of first family member: The first member of this family, AgrA, was identified in ''Pseudoalteromonas atlantica'' <cite>Belas1989</cite>. |
;First stereochemistry determination: not determined yet. | ;First stereochemistry determination: not determined yet. | ||
;First catalytic nucleophile identification: not determined yet. | ;First catalytic nucleophile identification: not determined yet. | ||
| Line 52: | Line 48: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Belas1989 pmid=2914859 |
| − | # | + | #Ohta2004 pmid=15490156 |
| − | # | + | #Ekborg2006 pmid=16672483 |
</biblio> | </biblio> | ||
Revision as of 02:17, 21 November 2010
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- 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
Glycoside hydrolases of family 86 are β-agarases (EC 3.2.1.81) that cleave β-1,4 glycosidic bonds of agarose. As of November 2010, only 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 [3].
Kinetics and Mechanism
A potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan GH-A enzymes. 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
- Identification of first family member
- The first member of this family, AgrA, was identified in Pseudoalteromonas atlantica [1].
- First stereochemistry determination
- not determined yet.
- First catalytic nucleophile identification
- not determined yet.
- First general acid/base residue identification
- not determined yet.
- First 3-D structure
- not determined yet.
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 |