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Difference between revisions of "Glycoside Hydrolase Family 136"
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|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |Asp |
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
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== Three-dimensional structures == | == Three-dimensional structures == | ||
[[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]] | [[file:LnbXc.png|thumb|300px|right|'''Figure 1: '''Overall structure of LnbXc with LNB (cyan) and two Ca2+ ions (orange).]] | ||
| − | [[file:ErGH136.png|thumb|300px|right|'''Figure | + | [[file:ErGH136.png|thumb|300px|right|'''Figure 2: '''Overall structure of ErGH136 with LNB (yellow).]] |
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>. | The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined <cite>chihaya2017</cite>. | ||
Revision as of 00:24, 3 March 2021
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- Author: ^^^Chihaya Yamada^^^
- Responsible Curator: ^^^Shinya Fushinobu^^^
| Glycoside Hydrolase Family GH136 | |
| Clan | GH-N |
| Mechanism | retaining |
| Active site residues | Asp |
| CAZy DB link | |
| https://www.cazy.org/GH136.html | |
Substrate specificities
This family of glycoside hydrolases contains lacto-N-biosidase, as demonstrated for LnbX from Bifidobacterium longum JCM 1217 [1]. LnbX liberates Galβ1-3GlcNAc(lacto-N-biose I, LNB) and lactose from lacto-N-tetraose, the main component of human milk oligosaccharides. It hydrolyzed the linkage GlcNAcβ1-3Gal in lacto-N-hexaose, lacto-N-fucopentaose I, and sialyllacto-N-tetraose a of human milk oligosaccharides as substrate of LnbX in the GH136. In addition, LnbX liberates Galβ1-3GalNAc (GNB) from the sugar chains of globo- and ganglio-series glycosphingolipids [2].
GH136 lacto-N-biosidase required neighboring chaperon gene for folding. Rarely, chaperone-like gene fused to lacto-N-biosidase gene in case of ErGH136I and ErGH136IIfrom Eubacterium ramulus [3].
Kinetics and Mechanism
LnbXc hydrolyzes the glycosidic linkage via a retaining mechanism involving a Grotthuss proton relay.
Catalytic Residues
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.
Three-dimensional structures
The X-ray crystal structure of the catalytic domain, LnbXc(31-625) revealed a right-handed β helix fold that is usually shared by polysaccharide active enzymes. Three forms, ligand free at 2.36 Å resolution (PDB ID 5GQC), LNB complex at 1.82 Å (PDB ID 5GQF), and GNB complex at 2.70 Å (PDB ID 5GQG) were determined [4]. The X-ray crystal structure of ErGH136 in complex with LNB (PDB ID 6KQT) revealed the N-terminal domain (ErLnb136I, from AA 7-224) consists of 8 α-helices (α1-α8) and Y145 of the α6-α7 loop positioned near the active site [3].
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
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- Error fetching PMID 23843461:
- Error fetching PMID 25839135:
- Error fetching PMID 32620774:
- Error fetching PMID 28392148: