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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 &beta;-agarases (EC [{{EClink}}3.2.1.81 3.2.1.81]) that cleave &beta;-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-&beta;-agarases <cite>REF1,REF2,REF3</cite>.
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To date, all characterized [[glycoside hydrolases]] of family 86 are &beta;-agarases (EC [{{EClink}}3.2.1.81 3.2.1.81]) that cleave &beta;-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'' <cite>REF1,REF2,REF3</cite>. AgaO from ''M. thermotolerans'' was reported to be an endo-hydrolytic enzyme, releasing neoagaro-hexaose as main product <cite>REF2</cite>, while the recombinant Aga86E from ''S. degradans'' released only neoagarobiose in an exo-acting manner.
  
  
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<biblio>
 
<biblio>
 
#REF1 pmid=2914859
 
#REF1 pmid=2914859
#REF2 pmid=15170112
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#REF2 pmid=15490156
 
#REF3 pmid=16672483
 
#REF3 pmid=16672483
  

Revision as of 05:12, 19 November 2010

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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

  1. 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 | PubMed ID:2914859 [REF1]
  2. 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 | PubMed ID:15490156 [REF2]
  3. 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 | PubMed ID:16672483 [REF3]

All Medline abstracts: PubMed