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Difference between revisions of "Glycoside Hydrolase Family 127"
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<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | ||
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* [[Author]]: ^^^Kiyotaka Fujita^^^ | * [[Author]]: ^^^Kiyotaka Fujita^^^ | ||
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^ | * [[Responsible Curator]]: ^^^Shinya Fushinobu^^^ | ||
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|'''Clan''' | |'''Clan''' | ||
| − | | | + | |none |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | This family of [[glycoside hydrolases]] contains β-L-arabinofuranosidase, which was recently established for HypBA1 from ''Bifidobacterium longum'' JCM 1217<cite>Fujita2011B</cite>. HypBA1 released L-arabinose from Ara''f''β1-2Ara''f'' (β-Ara<sub>2</sub>), Ara''f''β-hydroxyproline (Ara-Hyp), Ara''f''β1-2Ara''f''β-Hyp (Ara<sub>2</sub>-Hyp), Ara''f''β1-2Ara''f''β1-2Ara''f''β-hyp (Ara<sub>3</sub>-Hyp), methyl β-L-arabinofuranoside and Ara''f''β1-2Ara''f''β-Me, but not from from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The enzymes belonging to this family are also members of [http://pfam.sanger.ac.uk/family/DUF1680 Pfam DUF1680 family], conserved in many species of bacteria, actinomycetes, fugi, and plants. | + | This family of [[glycoside hydrolases]] contains β-L-arabinofuranosidase, which was recently established for HypBA1 from ''Bifidobacterium longum'' JCM 1217 <cite>Fujita2011B</cite>. HypBA1 released L-arabinose from Ara''f''β1-2Ara''f'' (β-Ara<sub>2</sub>), Ara''f''β-hydroxyproline (Ara-Hyp), Ara''f''β1-2Ara''f''β-Hyp (Ara<sub>2</sub>-Hyp), Ara''f''β1-2Ara''f''β1-2Ara''f''β-hyp (Ara<sub>3</sub>-Hyp), methyl β-L-arabinofuranoside and Ara''f''β1-2Ara''f''β-Me, but not from from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The enzymes belonging to this family are also members of [http://pfam.sanger.ac.uk/family/DUF1680 Pfam DUF1680 family], which is conserved in many species of bacteria, actinomycetes, fugi, and plants. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | HypBA1 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol, and produced methyl β-L-arabinofuranoside was identified by <sup>1</sup>H-NMR and <sup>13</sup>C-NMR analysis. | + | HypBA1 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol, and produced methyl β-L-arabinofuranoside was identified by <sup>1</sup>H-NMR and <sup>13</sup>C-NMR analysis <cite>Fujita2011B</cite>. |
== Catalytic Residues == | == Catalytic Residues == | ||
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== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: This was determined with HypBA1 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 HypBA1 enzyme by measurement of glycosyl transfer reactions to methanol and the <sup>1</sup>H-NMR and<sup>13</sup>C-NMR spectra <cite>Fujita2011B</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 03:30, 12 November 2012
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- Author: ^^^Kiyotaka Fujita^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
| Glycoside Hydrolase Family GH127 | |
| Clan | none |
| Mechanism | retaining |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/GH127.html | |
Substrate specificities
This family of glycoside hydrolases contains β-L-arabinofuranosidase, which was recently established for HypBA1 from Bifidobacterium longum JCM 1217 [1]. HypBA1 released L-arabinose from Arafβ1-2Araf (β-Ara2), Arafβ-hydroxyproline (Ara-Hyp), Arafβ1-2Arafβ-Hyp (Ara2-Hyp), Arafβ1-2Arafβ1-2Arafβ-hyp (Ara3-Hyp), methyl β-L-arabinofuranoside and Arafβ1-2Arafβ-Me, but not from from hydroxyproline-rich glycoproteins (HRGPs) such as carrot extensin and potato lectin. The enzymes belonging to this family are also members of Pfam DUF1680 family, which is conserved in many species of bacteria, actinomycetes, fugi, and plants.
Kinetics and Mechanism
HypBA1 is a retaining enzyme. The stereochemical course of the reaction was shown by transglycosylation activity toward 1-alkanols, such as methanol, and produced methyl β-L-arabinofuranoside was identified by 1H-NMR and 13C-NMR analysis [1].
Catalytic Residues
Not known.
Three-dimensional structures
Not known.
Family Firsts
- First stereochemistry determination
- This was determined with HypBA1 enzyme by measurement of glycosyl transfer reactions to methanol and the 1H-NMR and13C-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.
References
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Fujita K, Takashi Y, Obuchi E, Kitahara K, Suganuma T.(2011)Characterization of a novel β-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member. J Biol Chem. 286(44), 38079-85.[1]