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Difference between revisions of "Glycoside Hydrolase Family 121"
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* [[Author]]: ^^^Kiyotaka Fujita^^^ | * [[Author]]: ^^^Kiyotaka Fujita^^^ | ||
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^ | * [[Responsible Curator]]: ^^^Shinya Fushinobu^^^ | ||
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|'''Clan''' | |'''Clan''' | ||
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|'''Mechanism''' | |'''Mechanism''' | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | This family of [[glycoside hydrolases]] contains β-L-arabinobiosidase, which was recently established for HypBA2 from ''Bifidobacterium longum'' JCM 1217<cite>Fujita2011A</cite>. HypBA2 | + | This family of [[glycoside hydrolases]] contains β-L-arabinobiosidase, which was recently established for HypBA2 from ''Bifidobacterium longum'' JCM 1217 <cite>Fujita2011A</cite>. HypBA2 liberates Ara''f''β1-2Ara''f'' (β-Ara<sub>2</sub>) from unmodified Ara''f''β1-2Ara''f''β1-2Ara''f''β-hydroxyproline (Ara<sub>3</sub>-Hyp) but not Ara''f''α1-3Ara''f''β1-2Ara''f''β1-2Ara''f''β-Hyp (Ara<sub>4</sub>-Hyp) or Ara''f''β1-2Ara''f''β-Hyp (Ara<sub>2</sub>-Hyp). HypBA2 directly liberates β-Ara<sub>2</sub> from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The family members are only found from prokaryote genomes, such as bacteria and actinomycetes. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: This was determined with HypBA2 enzyme by measurement of glycosyl transfer reactions to methanol and the <sup>1</sup>H-NMR and <sup>13</sup>C-NMR spectra. | + | ;First stereochemistry determination: This was determined with HypBA2 enzyme by measurement of glycosyl transfer reactions to methanol and the <sup>1</sup>H-NMR and <sup>13</sup>C-NMR spectra <cite>Fujita2011A</cite>. |
;First catalytic nucleophile identification: No experimental proof. | ;First catalytic nucleophile identification: No experimental proof. | ||
;First general acid/base residue identification: No experimental proof. | ;First general acid/base residue identification: No experimental proof. | ||
Revision as of 03:26, 12 November 2012
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
- Author: ^^^Kiyotaka Fujita^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
| Glycoside Hydrolase Family GH121 | |
| Clan | none |
| Mechanism | retaining |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/GH121.html | |
Substrate specificities
This family of glycoside hydrolases contains β-L-arabinobiosidase, which was recently established for HypBA2 from Bifidobacterium longum JCM 1217 [1]. HypBA2 liberates Arafβ1-2Araf (β-Ara2) from unmodified Arafβ1-2Arafβ1-2Arafβ-hydroxyproline (Ara3-Hyp) but not Arafα1-3Arafβ1-2Arafβ1-2Arafβ-Hyp (Ara4-Hyp) or Arafβ1-2Arafβ-Hyp (Ara2-Hyp). HypBA2 directly liberates β-Ara2 from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The family members are only found from prokaryote genomes, such as bacteria and actinomycetes.
Kinetics and Mechanism
HypBA2 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol, and produced Arafβ1-2Arafβ-Me was identified by 1H-NMR and 13C-NMR analysis.
Catalytic Residues
Not known.
Three-dimensional structures
Not known.
Family Firsts
- First stereochemistry determination
- This was determined with HypBA2 enzyme by measurement of glycosyl transfer reactions to methanol and the 1H-NMR and 13C-NMR spectra [1].
- First catalytic nucleophile identification
- No experimental proof.
- First general acid/base residue identification
- No experimental proof.
- First 3-D structure
- Not known.