@ARTICLE{Eneyskaya1997173,
author={Eneyskaya, E.V. and Protasenya, S.V. and Kachurin, A.M. and Savel'ev, A.N. and Neustroev, K.N.},
title={Sh-group in the active site of α-galactosidase from Trichoderma reesei},
journal={Protein and Peptide Letters},
year={1997},
volume={4},
number={3},
pages={173-180},
note={cited By 3},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-2042484896&partnerID=40&md5=6a5132e7dc4d80d9494a48ce8297f9b2},
affiliation={Petersburg Nuclear Physics Institute, Molec./Radiat. Biophysics Division, Gatchina, St.Petersburg 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str., St.Petersburg, 195251, Russian Federation},
abstract={Modifications of an SH-group in active site of α-galactosidase from T. reesei by PHMB and Hg2+ inactivate the enzyme while following treatment with thiols activity is recovered. Galactose and substrates delay such recovery. This effect was utilized to compare affinity of substrates and galactose to native and inactive forms of the enzyme. It was concluded that the SH-group is important for binding of substrates in the active site.},
correspondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Molec./Radiat. Biophysics Division, Gatchina, St.Petersburg 188350, Russian Federation},
issn={09298665},
coden={PPELE},
language={English},
abbrev_source_title={Protein Pept. Lett.},
document_type={Article},
source={Scopus},
}

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