N-linked glycosylation influences on the catalytic and biochemical properties of Penicillium purpurogenum β-d-glucuronidase

Journal of Biotechnology

Volumn 157, Issue 3, 2012, Pages 399-404

  Zou, Shuping ^b   Xie, Luping ^a   Liu, Yanli ^a   Kaleem, Imdad ^a   Zhang, Guifeng ^c   Li, Chun ^a  

^a BEIJING INSTITUTE OF TECHNOLOGY   (China)

^b ZHEJIANG UNIVERSITY OF TECHNOLOGY   (China)

^c INSTITUTE OF PROCESS ENGINEERING   (China)

Author keywords

d Glucuronidase; Conformation; N glycosylation; Penicillium purpurogenum; Thermal stability

Indexed keywords

BIOCHEMICAL PROPERTIES; CONFORMATIONAL CHANGE; DEGLYCOSYLATION; DENATURATION TEMPERATURES; GLYCOSYLATED; GLYCYRRHIZIN; ISOFORMS; N-GLYCOSYLATION; N-LINKED; N-LINKED GLYCANS; N-LINKED GLYCOSYLATION; PENICILLIUM PURPUROGENUM; TERTIARY STRUCTURES;

CARBOHYDRATES; CONFORMATIONS; DIFFERENTIAL SCANNING CALORIMETRY; ENZYMES; ESTERIFICATION; FLUORESCENCE SPECTROSCOPY; GLYCOSYLATION; METAL IONS; THERMODYNAMIC STABILITY;

PLANTS (BOTANY);

BETA GLUCURONIDASE; CARBOHYDRATE; GLYCAN; GLYCYRRHIZIC ACID; METAL ION;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DEGLYCOSYLATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME CONFORMATION; ENZYME DENATURATION; FLUORESCENCE SPECTROSCOPY; GLYCOSYLATION; NONHUMAN; PENICILLIUM PURPUROGENUM; PRIORITY JOURNAL; TEMPERATURE MEASUREMENT; THERMOSTABILITY;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUCURONIDASE; GLYCOSYLATION; GLYCYRRHIZIC ACID; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; PENICILLIUM; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TEMPERATURE;

PENICILLIUM PURPUROGENUM;

EID: 84862796680     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.12.017     Document Type: Article

References (40)

1. Aiman F., Qayyum H. A role of glycosyl moieties in the stabilization of bitter gourd (Momordica charantia) peroxidase. Int. J. Biol. Macromol. 2007, 41:56-63.
2. Akao T. Competition in the metabolism of glycyrrhizin with glycyrrhetic acid mono-glucuronide by mixed Eubacterium sp. GLH and Ruminococcus sp. PO1-3. Biol. Pharm. Bull. 2000, 23:149-154.
3. Apweiler R., Hermjakob H., Sharon N.R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473:4-8.
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
5. Burda P., Aebi M. The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1999, 1426:239-257.
6. Chen M.M., Bartlett A.I., Nerenberg P.S., Friel C.T., Hackenberger C.P., Stultz C.M., Radford S.E., Imperiali B. Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:22528-22533.
7. Chen W., Hughes D.E., Bailey J.E. Intracellular expression of Vitreoscilla hemoglobin alters the aerobic metabolism of Saccharomyces cerevisiae. Biotechnol. Prog. 1994, 10:308-313.
8. Dalit S.B., Yaakov L. Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:8256-8261.
9. De G.J., Kosters H.A., De Jongh H.H.J. Deglycosylation of ovalbumin prohibits formation of a heat-stable conformer. Biotechnol. Bioeng. 2008, 97:735-741.
10. Desko M.M., Gross D.A., Kohler J.J. Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase. Glycobiology 2009, 10:1068-1077.
11. Escrevente C., Morais V.A., Keller S., Soares C.M., Altevogt P., Costa J. Functional role of N-glycosylation from ADAM 10 in processing, localization and activity of the enzyme. Biochim. Biophys. Acta 2008, 1780:905-913.
12. Feng S.J., Li C., Xu X.L., Wang X.Y. Screening strains for directed biosynthesis of β-d-mono-glucuronide-glycyrrhizin and kinetics of enzyme production. J. Mol. Catal. B: Enzym. 2006, 43:63-67.
13. Gemmill T.R., Trimble R.B. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1999, 1426:227-237.
14. Gopal B.A., Singh S.A., Muralikrishna G. Porcine pancreatic alpha amylase and its isoforms: effect of deglycosylation by peptide-N-glycosidase F. Int. J. Biol. Macromol. 2008, 43:100-105.
15. Haltiwanger R.S., Lowe J.B. Role of glycosylation in development. Biochemistry 2004, 73:491-537.
16. Imperiali B., O'Connor S.E. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 1999, 3:643-649.
17. Kim D.H., Lee K., Han K. Biotransformation of glycyrrhetinic acid-3-O-β-d-glucuronide by Streptococcus LJ-22, a human intestinal bacterium. Biol. Pharm. Bull. 1999, 22:320-322.
18. Koseki T., Yozo M., Mese Y., Miyanaga A., Fushinobu S., Wakagi T. Mutational analysis of N-glycosylation recognition sites on the biochemical properties of Aspergillus kawachii α-l-arabinofuranosidase 54. Biochim. Biophys. Acta 2006, 1760:1458-1464.
19. Kuramoto T., Ito Y., Oda M., Tamura Y., Kitahara S. Microbial production of glycyrrhetic acid 3-O-mono-β-d-glucuronide from glycyrrhizin by Cryptococcus magnus Mg-27. Biosci. Biotechnol. Biochem. 1994, 58:455-458.
20. Lis H., Sharon N. Protein glycosylation: structural and functional aspects. Eur. J. Biochem. 1993, 218:21-27.
21. Live D.H., Kumar A.R., Beebe X., Danishefsky S.J. Conformational influences of glycosylation of a peptide: a possible model for the effect of glycosylation on the rate of protein folding. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:12759-12761.
22. Manoel C.D.B., Roberto D.N.S., Marcelo H.S.R. The influence of N-glycosylation on biochemical properties of Amy1, an a-amylase from the yeast Cryptococcus flavus. Carbohydr. Res. 2009, 344:1682-1686.
23. Mer G., Hietter H., Lefevre J.F. Stabilization of proteins by glycosylation examined by NMR analysis on a fucosylated proteinase inhibitor. Nat. Struct. Biol. 1996, 3:45-53.
24. Mizutani K., Kambara T., Masuda H., Tamura Y. Glycyrrhetic acid monoglucuronide (MGGR): biological activities. Int. Congr. Ser. 1998, 1157:225-235.
25. Mizutani K., Kuramoto T., Tamura Y., Ohtake N., Shiqeki D., Nakura M. Sweetness of glycyrrhetic acid 3-O-β-d-monoglucuronide and the related glycosides. Biosci. Biotechnol. Biochem. 1994, 58:554-555.
26. Nelson D.L., Cox M.M. Biomolecules. Lehninger Principles of Biochemistry 2000, 53-78. Worth Publishers, New York. B. Geller (Ed.).
27. Patel V., Saunders G., Bucke C. Deglycosylation of fructosyltransferase and invertase from Fusarium oxysporum decreases stability but has little effect on kinetics and synthetic specificity. Biotechnol. Lett. 1997, 19:75-77.
28. Pham V.T., Ewing E., Kaplan H. Glycation improves the thermostability of trypsin and chymotrypsin. Biotechnol. Bioeng. 2008, 101:452-459.
29. Price J.L., Shental-Bechor D., Dhar A., Turner M.J., Powers E.T., Gruebele M., Levy Y., Kelly J.W. Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics. J. Am. Chem. Soc. 2010, 132:15359-15367.
30. Qi F., Dai D.Z., Liu Y.L., Kaleem I., Li C. Effects of low-shear modeled microgravity on the characterization of recombinant β-d-glucuronidase expressed in Pichia pastoris. Appl. Biochem. Biotechnol. 2010, 163:162-172.
31. Rudd P.M., Joao H.C., Coghill E., Fiten P., Saunders M.R., Opdenakker G., Dwek R.A. Glycoform modify the dynamic stability and functional activity of an enzyme. Biochemistry 1994, 33:17-22.
32. Somera A.F., Pereira M.G., Souza G.L.H., Polizeli M.L., Terenzi H.F., Melo F.R.P., Jorge J.A. Effect of glycosylation on the biochemical properties of beta-xylosidases from Aspergillus versicolor. J. Microbiol. 2009, 47:270-276.
33. Stahl C.H., Wilson D.B., Lei X.G. Comparison of extracellular Escherichia coli Appaphytases expressed in Streptomyces lividans and Pichia pastoris. Biotechnol. Lett. 2003, 25:827-831.
34. Tams J.W., Welinder K.G. Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase. Anal. Biochem. 1995, 228:48-55.
35. Velan B., Kronman C., Ordentlich A., Flashner Y., Leitner M., Cohen S., Shafferman A. N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis. Biochemistry 1993, 296:649-656.
36. Wei Y.D., Lee S.J., Lee K.S., Gui Z.Z., Yoon H.J., Kim I., Je Y.H., Guo X. N-glycosylation is necessary for enzymatic activity of a beetle (Apriona germari) cellulase. Biochem. Biophys. Res. Commun. 2005, 329:331-336.
37. Wyss M., Pasamontes L., Friedlein A., Rémy R., Tessier M., Kronenberger A., Middendorf A., Lehmann M., Schnoebelen L., Röthlisberger U., Kusznir E., Wahl G., Müller F., Lahm H.W., Vogel K., van Loon A.P.G.M. Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance. Appl. Environ. Microbiol. 1999, 65:359-366.
38. Yanez E., Carmona T.A., Tiemblo M., Jimenez A., Fernandez-Lobato M. Expression of the Schwanniomyces occidentalis SWA2 amlyase in Saccharomyces cerevisiae: role of N-glycosylation on activity, stability and secretion. Biochem. J. 1998, 329:65-71.
39. Yoshimasu M.A., Tanaka T., Ahn J.K., Yada R.Y. Effect of N-linked glycosylation on the aspartic proteinase porcine pepsin expressed from Pichia pastoris. Glycobiology 2004, 14:417-429.
40. Yuka M., Satoshi T., Seiya M. The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation. Biochim. Biophys. Acta 2010, 1804:156-165.