Polysaccharide epimerases

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• Author: ^^^Margrethe Gaardlos^^^ and ^^^Anne Tondervik^^^
• Responsible Curator: ^^^Finn Aachmann^^^

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Introduction

Substrate specificities

Mannuronan C5-epimerases are a group of enzymes that catalyze epimerization at the polymer-level of β-d-mannuronic acid residues (hereafter denoted M) into α-l-guluronic acid residues (hereafter denoted G) in alginate [1, 2, 3]. Alginate is an anionic polysaccharide made by brown seaweeds, some species of red algae, and the gram-negative bacterial genera Pseudomonas and Azotobacter [4, 5, 6, 7, 8]. The function of alginate in the different organisms are various, and related to structure, protection and surface adhesion [9, 10, 11, 12]. Alginate is a copolymer of the two 1-4 linked epimers [13, 14, 15], and by changing the composition of the two monomers the epimerases fine-tune the properties of the polymer [16].

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References

1. 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 |
2. 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 |
3. 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 |

4. 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

5. 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]

6. 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
7. 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 |

8. 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]

9. Painter, Terence J. (1983) Chapter 4 - Algal Polysaccharides. Edited by Gerald O. Aspinall. The Polysaccharides. New York: Academic Press. [1]

10. Campos M, Martínez-Salazar JM, Lloret L, Moreno S, Núñez C, Espín G, and Soberón-Chávez G. (1996). Characterization of the gene coding for GDP-mannose dehydrogenase (algD) from Azotobacter vinelandii. J Bacteriol. 1996;178(7):1793-9. DOI:10.1128/jb.178.7.1793-1799.1996 |
11. Pier GB, Coleman F, Grout M, Franklin M, and Ohman DE. (2001). Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis. Infect Immun. 2001;69(3):1895-901. DOI:10.1128/IAI.69.3.1895-1901.2001 |
12. Harmsen M, Yang L, Pamp SJ, and Tolker-Nielsen T. (2010). An update on Pseudomonas aeruginosa biofilm formation, tolerance, and dispersal. FEMS Immunol Med Microbiol. 2010;59(3):253-68. DOI:10.1111/j.1574-695X.2010.00690.x |

13. Hirst, E. L. and Jones, J. K. N and Jones, Winifred Osman. (1939) 389. The structure of alginic acid. Part I [in en]. Journal of the Chemical Society, The Royal Society of Chemistry. Vol. 0, pp. 1880–1885. [1]

14. FISCHER FG and DORFEL H. (1955). [Polyuronic acids in brown algae]. Hoppe Seylers Z Physiol Chem. 1955;302(4-6):186-203. | Google Books | Open Library

15. Drummond, D W and Hirst, E L and Percival, Elizabeth. (1962) 232. The constitution of alginic acid. Journal of the Chemical Society, The Royal Society of Chemistry. Vol. 0, pp. 1208–1216. [1]

16. Ertesvåg H, Høidal HK, Schjerven H, Svanem BI, and Valla S. (1999). Mannuronan C-5-epimerases and their application for in vitro and in vivo design of new alginates useful in biotechnology. Metab Eng. 1999;1(3):262-9. DOI:10.1006/mben.1999.0130 |
17. 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 |

18. 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.