Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei. Eneyskaya, E., Sundqvist, G., Golubev, A., Ibatullin, F., Ivanen, D., Shabalin, K., Brumer, H., & Kulminskaya, A. Biochimie, 91(5):632-638, 2009. cited By 18Paper doi abstract bibtex A purified β-mannosidase (EC 3.2.1.25) from the fungus Trichoderma reesei has been identified as a member of glycoside hydrolase family 2 through mass spectrometry analysis of tryptic peptides. In addition to hydrolysis, the enzyme catalyzes substrate transglycosylation with p-nitrophenyl β-mannopyranoside. Structures of the major and minor products of this reaction were identified by NMR analysis as p-nitrophenyl mannobiosides and p-nitrophenyl mannotriosides containing β-(1 → 4) and β-(1 → 3) linkages. The rate of donor substrate hydrolysis increased in presence of acetonitrile and dimethylformamide, while transglycosylation was weakly suppressed by these organic solvents. Differential ultraviolet spectra of the protein indicate that a rearrangement of the hydrophobic environment of the active site following the addition of the organic solvents may be responsible for this hydrolytic activation. © 2009 Elsevier Masson SAS. All rights reserved.
@ARTICLE{Eneyskaya2009632,
author={Eneyskaya, E.V. and Sundqvist, G. and Golubev, A.M. and Ibatullin, F.M. and Ivanen, D.R. and Shabalin, K.A. and Brumer, H. and Kulminskaya, A.A.},
title={Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei},
journal={Biochimie},
year={2009},
volume={91},
number={5},
pages={632-638},
doi={10.1016/j.biochi.2009.03.009},
note={cited By 18},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-64049097092&doi=10.1016%2fj.biochi.2009.03.009&partnerID=40&md5=2eb0f1a7d4883969c402b5c2be2284dd},
affiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biophysics Division, Orlova Roscha, Gatchina, 188300 Leningrad District, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, 106 91 Stockholm, Sweden},
abstract={A purified β-mannosidase (EC 3.2.1.25) from the fungus Trichoderma reesei has been identified as a member of glycoside hydrolase family 2 through mass spectrometry analysis of tryptic peptides. In addition to hydrolysis, the enzyme catalyzes substrate transglycosylation with p-nitrophenyl β-mannopyranoside. Structures of the major and minor products of this reaction were identified by NMR analysis as p-nitrophenyl mannobiosides and p-nitrophenyl mannotriosides containing β-(1 → 4) and β-(1 → 3) linkages. The rate of donor substrate hydrolysis increased in presence of acetonitrile and dimethylformamide, while transglycosylation was weakly suppressed by these organic solvents. Differential ultraviolet spectra of the protein indicate that a rearrangement of the hydrophobic environment of the active site following the addition of the organic solvents may be responsible for this hydrolytic activation. © 2009 Elsevier Masson SAS. All rights reserved.},
author_keywords={β-Mannosidase; Organic solvents; p-Nitrophenyl β-mannooligosaccharides; Transglycosylation},
funding_details={Российский Фонд Фундаментальных Исследований (РФФИ)07-04-01071-a},
}
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