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Difference between revisions of "Polysaccharide Lyase Family 19"

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(Created page with '* Responsible Curator: ^^^Bernard Henrissat^^^ ---- === PL19 is a deleted family === ==== History ==== Entries in Glycoside Hydrolase Family 91 were originally reclassif…')
 
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* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
 
* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
 
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=== PL19 is a deleted family ===
 
==== History ====
 
Entries in [[Glycoside Hydrolase Family 91]] were originally reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction.  Indeed, polysaccharide cleavage occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]).
 
 
The family was re-reclassified as [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]].  Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family.
 
  
 
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=== PL19 is a deleted family ===
 +
==== History ====
 +
Entries in [[Glycoside Hydrolase Family 91]] were originally reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction.  Indeed, polysaccharide cleavage occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]).
 +
 +
The family was re-reclassified as [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]].  Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family <cite>Sakurai1997 Saito2003</cite>.
 +
 +
==== References ====
 +
<biblio>
 +
#Sakurai1997 H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. [http://dx.doi.org/10.1271/bbb.61.989 DOI: 10.1271/bbb.61.989]
 +
#Saito2003 pmid=16233453
 +
</biblio>
 +
  
 
{{CuratorApproved}}
 
{{CuratorApproved}}
 
[[Category:Polysaccharide Lyase Families|GH091]]
 
[[Category:Polysaccharide Lyase Families|GH091]]
 
[[Category:Deleted families]]
 
[[Category:Deleted families]]

Revision as of 01:23, 20 April 2010


CAZy DB links
http://www.cazy.org/fam/GH91.html
http://www.cazy.org/fam/PL19.html

PL19 is a deleted family

History

Entries in Glycoside Hydrolase Family 91 were originally reclassified to Polysaccharide Lyase Family 19 on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC 4.2.2.17 and EC 4.2.2.18).

The family was re-reclassified as Glycoside Hydrolase Family 91 on 20 April 2010 due to direct analogy with the lytic transglycosidases of GH23, GH102, GH103, and GH104. Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family [1, 2].

References

  1. H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. DOI: 10.1271/bbb.61.989

    [Sakurai1997]
  2. Saito K, Sumita Y, Nagasaka Y, Tomita F, and Yokota A. (2003). Molecular cloning of the gene encoding the di-D-Fructofuranose 1,2':2,3' dianhydride hydrolysis enzyme (DFA IIIase) from Arthrobacter sp. H65-7. J Biosci Bioeng. 2003;95(5):538-40. DOI:10.1016/s1389-1723(03)80058-0 | PubMed ID:16233453 [Saito2003]


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