Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity

Bioorganic and Medicinal Chemistry

Volumn 8, Issue 7, 2000, Pages 1537-1544

  Lloyd, Richard C ^a   Davis, Benjamin G ^b   Jones, J Bryan ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b DURHAM UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE; SERINE PROTEINASE; SUBTILISIN;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DEACYLATION; EGGERTHELLA LENTA; ENZYME ACTIVE SITE; ENZYME ACTIVITY; METHODOLOGY; MICHAELIS MENTEN KINETICS; MOLECULAR MODEL; NONHUMAN; PROTEIN GLYCOSYLATION;

ACETYLATION; AMIDOHYDROLASES; BACILLUS; BINDING SITES; COMBINATORIAL CHEMISTRY TECHNIQUES; ESTERASES; GLYCOPROTEINS; GLYCOSYLATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; STRUCTURE-ACTIVITY RELATIONSHIP; SUBTILISIN;

BACILLUS LENTUS; FELIS CATUS;

EID: 0033917398     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(00)00084-5     Document Type: Article

References (11)

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9. 3 (0.15 mM) is evidently so small that the approximation does not hold in this case.
10. While the substrate employed for kinetic analysis is succinylated, we did not include this moiety in molecular modeling since its orientation was not reported in the X-ray structure of SBL, suggesting high mobility in the crystal.
11. Biosym Technologies, Inc., San Diego, CA, USA.