Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei

Biochimie

Volumn 91, Issue 5, 2009, Pages 632-638

  Eneyskaya, Elena V ^a   Sundqvist, Gustav ^b   Golubev, Alexander M ^a   Ibatullin, Farid M ^a   Ivanen, Dina R ^a   Shabalin, Konstantin A ^a   Brumer, Harry ^b   Kulminskaya, Anna A ^a  

^a PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^b ALBANOVA UNIVERSITY CENTER   (Sweden)

Author keywords

Mannosidase; Organic solvents; p Nitrophenyl mannooligosaccharides; Transglycosylation

Indexed keywords

ACETONITRILE; BETA MANNOSIDASE; MANNOSIDE; N,N DIMETHYLFORMAMIDE; PYRANOSIDE;

ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME SUBSTRATE; HYDROLYSIS; HYDROPHOBICITY; NUCLEOTIDE SEQUENCE; TRICHODERMA REESEI;

BETA-MANNOSIDASE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; FUNGAL PROTEINS; GLYCOSYLATION; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TRICHODERMA; TRYPSIN;

FUNGI; HYPOCREA JECORINA;

EID: 64049097092     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.03.009     Document Type: Article

References (36)

1. Pérez J., Muñoz-Dorado J., de la Rubia T., and Martínez J. Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview. Int. Microbiol. 5 (2002) 53-63
2. Karboune S., Geraert P.A., and Kermasha S. Characterization of selected cellulolytic activities of multi-enzymatic complex system from Penicillium funiculosum. J. Agric. Food Chem. 56 (2008) 903-909
3. Zverlov V.V., and Schwarz W.H. Bacterial cellulose hydrolysis in anaerobic environmental subsystems - Clostridium thermocellum and Clostridium stercorarium, thermophilic plant-fiber degraders. Ann. N.Y. Acad. Sci. 1125 (2008) 298-307
4. Pason P., Kyu K.L., and Ratanakhanokchai K. Paenibacillus curdlanolyticus strain B-6 xylanolytic-cellulolytic enzyme system that degrades insoluble polysaccharides. Appl. Environ. Microbiol. 72 (2006) 2483-2490
5. Béra-Maillet C., Ribot Y., and Forano E. Fiber-degrading systems of different strains of the genus Fibrobacter. Appl. Environ. Microbiol. 70 (2004) 2172-2179
6. Azuma J.I., and Koshijima T. Enzymatic saccharification of woody plants. II. Synergistic effects on enzymatic saccharification. Wood Res. 70 (1984) 17-24
7. Gilbert H.J., Stålbrand H., and Brumer H. How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr. Opin. Plant Biol. 11 (2008) 338-348
8. Tailford L.E., Money V.A., Smith N.L., Dumon C., Davies G.J., and Gilbert H.J. Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the β-mannosidase, BtMan2A. J. Biol. Chem. 282 (2007) 11291-11299
9. Zhu M., Lovell K.L., Patterson J.S., Saunders T.L., Hughes E.D., and Friderici K.H. β-Mannosidosis mice: a model for the human lysosomal storage disease. Hum. Mol. Genet. 15 (2006) 493-500
10. Percheron F., Foglietti M.J., Bernard M., and Ricard B. Mammalian β-d-mannosidase and β-mannosidosis. Biochimie 74 (1992) 5-11
11. Uchino Y., Fukushige T., Yotsumoto S., Hashiguchi T., Taguchi H., Suzuki N., Konohana I., and Kanzaki T. Morphological and biochemical studies of human β-mannosidosis: identification of a novel β-mannosidase gene mutation. Br. J. Dermatol. 149 (2003) 23-29
12. Cantarel B.L., Coutinho P.M., Rancurel C., Bernard T., Lombard V., and Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37 (2009) D233-D238
13. Codée J.D.C., Hossain L.H., and Seeberger P.H. Efficient installation of β-mannosides using a dehydrative coupling strategy. Org. Lett. 7 (2005) 3251-3254
14. Crich D., Li W., and Li H. Direct chemical synthesis of the β-mannans: linear and block syntheses of the alternating β-(1 → 3)-β-(1 → 4)-mannan common to Rhodotorula glutinis, Rhodotorula mucilaginosa, and Leptospira biflexa. J. Am. Chem. Soc. 126 (2004) 15081-15086
15. Kyosaka S., Murata S., Tsuda Y., and Tanaka M. Isolation and identification of self-transfer products formed by guinea pig liver β-mannosidase. Chem. Pharm. Bull. 34 (1986) 5140-5143
16. Singh M.S., and Crout D.H.G. Glycosidase catalyzed synthesis of oligosaccharides: two-step synthesis of the core trisaccharide of N-linked glycoproteins using the β-N-acetylhexosaminidase and the β-mannosidase from Aspergillus oryzae. Chem. Commun. (1996) 993-994
17. Scigelova M., Singh S., and Crout D.H.G. Purification of the β-N-acetylhexosaminidase from Aspergillus oryzae and the β-mannosidases from Helix pomatia and A. oryzae and their application to the enzymatic synthesis of the core trisaccharide of the N-linked glycoproteins. J. Chem. Soc. Perkin Trans. 1 (1999) 777-782
18. Usui, Suzuki M., Sato T., Kawagishi H., Adachi K., and Sano H. Enzymic synthesis of the trisaccharide core region of the carbohydrate chain of N-glycoprotein. Glycoconj. J. 11 (1994) 105-110
19. Kulminskaya A.A., Eneyskaya E.V., Isaeva-Ivanova L.S., Savel'ev A.N., Sidorenko I.A., Savel'ev A.N., Shabalin K.A., Golubev A.M., and Neustroev K.N. Enzymatic activity and beta-galactomannan binding property of β-mannosidase from Trichoderma reesei. Enzyme Microb. Technol. 25 (1999) 372-377
20. Aparicio R., Fischer H., Scott D.J., Verschueren K.H.G., Kulminskaya A.A., Eneiskaya E.V., Neustroev K.N., Graevich A.F., Golubev A.M., and Polikarpov I. Structural insights into the β-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography. Biochemistry 41 (2002) 9370-9375
21. Kinter M., and Sherman N.E. An in-gel digestion protocol. In: Desiderio D.M., and Nibbering N.M.M. (Eds). Protein Sequencing and Identification Using Tandem Mass Spectrometry, the Preparation of Protein Digests for Mass Spectrometric Sequencing Experiments (2005), John Wiley & Sons, Inc. 153-157
22. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215 (1990) 403-410
23. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
24. Eswar N., Webb B., Marti-Renom M.A., Madhusudhan M.S., Eramian D., Shen M.Y., Pieper U., and Sali A. Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. 2.9 (2007) (Chapter 2)
25. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst 24 (1991) 946-950
26. Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524
27. Jacobson R.H., Zhang X.J., DuBose R.F., and Matthews B.W. Three-dimensional structure of β-galactosidase from E. coli. Nature 369 (1994) 761-766
28. Jain S., Drendel W.B., Chen Z.W., Mathews F.S., Sly W.S., and Grubb J.H. Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat. Struct. Biol. 3 (1996) 375-381
29. 1H n.m.r. determination of the stereochemical course of hydrolyses catalysed by glucanase components of the cellulase complex. Biochem. Biophys. Res. Commun. 139 (1986) 487-494
30. Côté N., Fleury A., Dumont-Blanchette E., Fukamizo T., Mitsutomi M., and Brzezinski R. Two exo-β-d-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem. J. 394 (2006) 675-686
31. Andreotti G., Giordano A., Tramice A., Mollo E., and Trincone A. Purification and characterization of a β-d-mannosidase from the marine anaspidean Aplysia fasciata. J. Biotechnol. 119 (2005) 26-35
32. Akaike E., Tsutsumida M., Osumi K., Fujita M., Yamanoi T., Yamamoto K., and Fujita K. High efficiency of transferring a native sugar chain from a glycopeptide by a microbial endoglycosidase in organic solvents. Carbohydr. Res. 339 (2004) 719-722
33. Oikawa T., Tsukagawa Y., Chino M., and Soda K. Increased transglycosylation activity of Rhodotorula glutinis endo-β-glucanase in media containing organic solvent. Biosci. Biotechnol. Biochem. 65 (2001) 1889-1892
34. Donovan J.W. Changes in ultraviolet absorption produced by alteration of protein conformation. J. Biol. Chem. 244 (1969) 1961-1967
35. Hong J., Tamaki H., and Kumagai H. Unusual hydrophobic linker region of β-glucosidase (BGLII) from Thermoascus aurantiacus is required for hyper-activation by organic solvents. Appl. Microbiol. Biotechnol. 73 (2006) 80-88
36. Marti-Renom M.A., Stuart A., Fiser A., Sánchez R., Melo F., and Sali A. Comparative protein structure modeling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 291-325