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Difference between revisions of "Polysaccharide epimerases"
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* Responsible Curator: ^^^Finn Aachmann^^^ | * Responsible Curator: ^^^Finn Aachmann^^^ | ||
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− | == | + | == Introduction == |
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− | In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. | + | <!--In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.--> |
− | === | + | === Substrate specificities === |
− | '' | + | <!-- Mannuronan C5-epimerases are a group of enzymes that catalyze epimerization at the polymer-level of β-<font style="font-feature-settings: 'smcp'">d</font>-mannuronic acid residues (hereafter denoted M) into α-<font style="font-feature-settings: 'smcp'">l</font>-guluronic acid residues (hereafter denoted G) in alginate <cite>haug1969, larsen1971, haug1971</cite>. Alginate is an anionic polysaccharide made by brown seaweeds, some species of red algae, and the gram-negative bacterial genera ''Pseudomonas'' and ''Azotobacter'' <cite>Stanford1883, Gorin1966, Linker1966, govan1981, okazaki1982</cite>. The function of alginate in the different organisms are various, and related to structure, protection and surface adhesion \autocite{painter1983, campos1996, Pier2001, Harmsen2010}. Alginate is a copolymer of the two 1-4 linked epimers \autocite{Hirst1939, fischer1955, Drummond1962}, and by changing the composition of the two monomers the epimerases fine-tune the properties of the polymer \autocite{Ertesvaag1999}. --> |
− | === | + | === Classification === |
− | + | ||
+ | === Product profiles === | ||
+ | <!-- ====Sub-subsection==== --> | ||
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== Main section 2 == | == Main section 2 == | ||
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#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]. | ||
+ | #haug1969 pmid=5368261 | ||
+ | #larsen1971 pmid=5150891 | ||
+ | #haug1971 pmid=5150892 | ||
+ | #Stanford1883 Stanford, Edw C C. (1883) On algin: a new substance obtained from some of the commoner species of marine algae. R. Anderson. NLM ID: 101217546 | ||
+ | #Gorin1966 Gorin, P. A. J. and Spencer, J. F. T. (1966) Exocellular alginic acid from ''Azotobacter vinelandii''. ''Canadian Journal of Chemistry'' vol. 44, no. 9., pp. 993-998. [https://www.nrcresearchpress.com/doi/abs/10.1139/v66-147#citart1] | ||
+ | #Linker1966 pmid=5916397 | ||
+ | #govan1981 pmid=6801192 | ||
+ | #okazaki1982 Okazaki, M., K. and Furuya, K. Tsukayam and K. Nisizawa. (1982) Isolation and Identification of Alginic Acid from a Calcareous Red Alga ''Serraticardia maxima''. ''Botanica Marina'', vol. 25, no. 3., pp. 123-131. [https://www.degruyter.com/view/journals/botm/25/3/article-p123.xml] | ||
+ | |||
</biblio> | </biblio> | ||
− | |||
[[Category:Definitions and explanations]] | [[Category:Definitions and explanations]] |
Revision as of 23:57, 7 April 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: ^^^Margrethe Gaardlos^^^ and ^^^Anne Tondervik^^^
- Responsible Curator: ^^^Finn Aachmann^^^
Introduction
Substrate specificities
Classification
Product profiles
Main section 2
Whatevs...
References
- 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.
- Haug A and Larsen B. (1969). Biosynthesis of alginate. Epimerisation of D-mannuronic to L-guluronic acid residues in the polymer chain. Biochim Biophys Acta. 1969;192(3):557-9. DOI:10.1016/0304-4165(69)90414-0 |
- Larsen B and Haug A. (1971). Biosynthesis of alginate. 1. Composition and structure of alginate produced by Azotobacter vinelandii (Lipman). Carbohydr Res. 1971;17(2):287-96. DOI:10.1016/s0008-6215(00)82536-7 |
- Haug A and Larsen B. (1971). Biosynthesis of alginate. II. Polymannuronic acid C-5-epimerase from Azotobacter vinelandii (Lipman). Carbohydr Res. 1971;17(2):297-308. DOI:10.1016/s0008-6215(00)82537-9 |
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Stanford, Edw C C. (1883) On algin: a new substance obtained from some of the commoner species of marine algae. R. Anderson. NLM ID: 101217546
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Gorin, P. A. J. and Spencer, J. F. T. (1966) Exocellular alginic acid from Azotobacter vinelandii. Canadian Journal of Chemistry vol. 44, no. 9., pp. 993-998. [1]
- Linker A and Jones RS. (1966). A new polysaccharide resembling alginic acid isolated from pseudomonads. J Biol Chem. 1966;241(16):3845-51. | Google Books | Open Library
- Govan JR, Fyfe JA, and Jarman TR. (1981). Isolation of alginate-producing mutants of Pseudomonas fluorescens, Pseudomonas putida and Pseudomonas mendocina. J Gen Microbiol. 1981;125(1):217-20. DOI:10.1099/00221287-125-1-217 |
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Okazaki, M., K. and Furuya, K. Tsukayam and K. Nisizawa. (1982) Isolation and Identification of Alginic Acid from a Calcareous Red Alga Serraticardia maxima. Botanica Marina, vol. 25, no. 3., pp. 123-131. [1]