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New to the CAZy classification? Read this first.
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Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
Difference between revisions of "Auxiliary Activity Family 5"
| Line 42: | Line 42: | ||
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | AA5 share a seven-bladed β-propeller fold <cite>Ito1994,Yin2015,Mathieu202</cite> as the catalytic domain containing the active site. | |
== Family Firsts == | == Family Firsts == | ||
| Line 52: | Line 52: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | #Cantarel2009 pmid=18838391 | + | |
| + | # Whittaker1996 pmid= 8557673 | ||
| + | |||
| + | #Whittaker2003 pmid= 12797833 | ||
| + | |||
| + | #Andberg2017 pmid=28778886 | ||
| + | |||
| + | #Yin2015 pmid= 26680532 | ||
| + | |||
| + | #Oide2019 pmid= 30885320 | ||
| + | |||
| + | #Mathieu2020 Mathieu, Y., Offen, W. A., Forget, S. M., Ciano, L., Viborg, A. H., Blagova, E., Henrissat, B., Walton, P.H, Davies, G.J, and Brumer, H. (2020). Discovery of a fungal copper radical oxidase with high catalytic efficiency toward 5-hydroxymethylfurfural and benzyl alcohols for bioprocessing. ACS Catalysis, 10(5), 3042-3058. https://pubs.acs.org/doi/abs/10.1021/acscatal.9b04727 | ||
| + | |||
| + | #Kersten1987 pmid= 3553159 | ||
| + | |||
| + | #Ogel1994 Ögel, Z. B.; Brayford, D.; McPherson, M. J., (1994). Cellulose-triggered sporulation in the galactose oxidase-producing fungus Cladobotryum (Dactylium) dendroides NRRL 2903 and its re-identification as a species of Fusarium. Mycol. Res., 98 (4), 474-480. https://doi.org/10.1016/j.pep.2014.12.010 | ||
| + | |||
| + | #Cooper1959 pmid= 13641238 | ||
| + | |||
| + | #Amaral1963 pmid= 14012475 | ||
| + | |||
| + | #Cleveland2021a pmid=34134727 | ||
| + | |||
| + | #Paukner2014 PMID=24967652 | ||
| + | |||
| + | #Paukner2015 PMID=25543085 | ||
| + | |||
| + | #Faria2019 PMID=31177409#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. [https://doi.org/10.1042/BIO03004026 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. [https://doi.org/10.1042/BIO03004026 Download PDF version]. | ||
</biblio> | </biblio> | ||
[[Category:Auxiliary Activity Families|AA005]] | [[Category:Auxiliary Activity Families|AA005]] | ||
Revision as of 15:09, 9 September 2021
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: ^^^Maria Cleveland^^^ and ^^^Yann Mathieu^^^
- Responsible Curator: ^^^Harry Brumer^^^
| Auxiliary Activity Family AA5 | |
| Fold | Seven-bladed β-propeller |
| Mechanism | Copper Radical Oxidase |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/AA5.html | |
Substrate specificities
Content is to be added here.
Authors may get an idea of what to put in each field from Curator Approved Auxiliary Activity Families and 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
AA5 share a seven-bladed β-propeller fold [3, 4, 5] as the catalytic domain containing the active site.
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
-
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.
-
pmid= 26680532
-
pmid= 8557673
-
pmid= 12797833
- Andberg M, Mollerup F, Parikka K, Koutaniemi S, Boer H, Juvonen M, Master E, Tenkanen M, and Kruus K. (2017). A Novel Colletotrichum graminicola Raffinose Oxidase in the AA5 Family. Appl Environ Microbiol. 2017;83(20). DOI:10.1128/AEM.01383-17 |
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pmid= 30885320
-
Mathieu, Y., Offen, W. A., Forget, S. M., Ciano, L., Viborg, A. H., Blagova, E., Henrissat, B., Walton, P.H, Davies, G.J, and Brumer, H. (2020). Discovery of a fungal copper radical oxidase with high catalytic efficiency toward 5-hydroxymethylfurfural and benzyl alcohols for bioprocessing. ACS Catalysis, 10(5), 3042-3058. https://pubs.acs.org/doi/abs/10.1021/acscatal.9b04727
-
pmid= 3553159
-
Ögel, Z. B.; Brayford, D.; McPherson, M. J., (1994). Cellulose-triggered sporulation in the galactose oxidase-producing fungus Cladobotryum (Dactylium) dendroides NRRL 2903 and its re-identification as a species of Fusarium. Mycol. Res., 98 (4), 474-480. https://doi.org/10.1016/j.pep.2014.12.010
-
pmid= 13641238
-
pmid= 14012475
- Cleveland M, Lafond M, Xia FR, Chung R, Mulyk P, Hein JE, and Brumer H. (2021). Two Fusarium copper radical oxidases with high activity on aryl alcohols. Biotechnol Biofuels. 2021;14(1):138. DOI:10.1186/s13068-021-01984-0 |
-
PMID=24967652
-
PMID=25543085
-
PMID=31177409#Cantarel2009 pmid=18838391