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Difference between revisions of "Glycoside Hydrolase Family 137"
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== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | The structure of BT0996 comprises a single domain which is a five bladed β-propeller fold. Each blade is composed of three to four anti parallel β-strands that extend out radially from the central core. The final blade is formed by strands from both the N- and C-terminus of the protein which is termed as 'molecular velcro' and is believed to add considerable stability to the fold. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not Known. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile/base identification: Inferred to be Glu159 in BT0996 <cite>Ndeh2017</cite>. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Inferred to be Glu240 in BT0996<cite>Ndeh2017</cite>. |
| − | ;First 3-D structure: | + | ;First 3-D structure: The first structure determination for GH137 was of BT0996 from the organism ''Bacteroides thetaiotaomicon''<cite>Ndeh2017</cite>. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| + | #Ndeh2017 pmid=28329766 | ||
#Cantarel2009 pmid=18838391 | #Cantarel2009 pmid=18838391 | ||
#DaviesSinnott2008 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. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | #DaviesSinnott2008 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. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | ||
Revision as of 07:28, 25 January 2020
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.
- Author: ^^^Alan Cartmell^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| Glycoside Hydrolase Family GH137 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH137.html | |
Substrate specificities
Content is to be added here.
Authors may get an idea of what to put in each field from Curator Approved Glycoside Hydrolase Families. (TIP: Right click with your mouse and open this link in a new browser window...)
In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
The structure of BT0996 comprises a single domain which is a five bladed β-propeller fold. Each blade is composed of three to four anti parallel β-strands that extend out radially from the central core. The final blade is formed by strands from both the N- and C-terminus of the protein which is termed as 'molecular velcro' and is believed to add considerable stability to the fold.
Family Firsts
- First stereochemistry determination
- Not Known.
- First catalytic nucleophile/base identification
- Inferred to be Glu159 in BT0996 [3].
- First general acid/base residue identification
- Inferred to be Glu240 in BT0996[3].
- First 3-D structure
- The first structure determination for GH137 was of BT0996 from the organism Bacteroides thetaiotaomicon[3].
References
-
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.
- 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 |
- Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 |