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Difference between revisions of "Carbohydrate Esterase Family 20"
| Line 32: | Line 32: | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | The caracterized members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families, but this inference still requires experimental validation. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database <cite>Cantarel2009</cite>) in the α5-η3 loop . | + | The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop . |
== Family Firsts == | == Family Firsts == | ||
Revision as of 09:17, 22 March 2023
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
| Carbohydrate Esterase Family CE20 | |
| Fold | β-sandwich/(α-β-α) sandwich/β-sandwich |
| Mechanism | serine hydrolase |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/CE20.html | |
Substrate specificities
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases [1] and acetylesterases putatively related to arabinoxylan deacetylation [2] .
Kinetics and Mechanism
XacXaeA, the founding member of family CE20 [1], harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family CE1. However, this assumption still requires experimental validation.
Catalytic Residues
The caracterized members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families, but this inference still requires experimental validation.
Three-dimensional structures
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure [1]. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 [1], the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database [3, 4]) in the α5-η3 loop .
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
- Xanthomonas citri subsp. citri 306 xyloglucan acetylesterase crystal structure in 2021 [1].
References
- Vieira PS, Bonfim IM, Araujo EA, Melo RR, Lima AR, Fessel MR, Paixão DAA, Persinoti GF, Rocco SA, Lima TB, Pirolla RAS, Morais MAB, Correa JBL, Zanphorlin LM, Diogo JA, Lima EA, Grandis A, Buckeridge MS, Gozzo FC, Benedetti CE, Polikarpov I, Giuseppe PO, and Murakami MT. (2021). Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors. Nat Commun. 2021;12(1):4049. DOI:10.1038/s41467-021-24277-4 |
- Liu N, Gagnot S, Denis Y, Byrne D, Faulds C, Fierobe HP, and Perret S. (2022). Selfish uptake versus extracellular arabinoxylan degradation in the primary degrader Ruminiclostridium cellulolyticum, a new string to its bow. Biotechnol Biofuels Bioprod. 2022;15(1):127. DOI:10.1186/s13068-022-02225-8 |
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.