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Volumn 96, Issue 5, 2011, Pages 1009-1014
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Why substituting the asparagine at position 35 in Bacillus circulans xylanase with an aspartic acid remarkably improves the enzymatic catalytic activity? A quantum chemistry-based calculation study
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Author keywords
Asparagine; Aspartic acid; Catalytic mechanism; DFT; Xylanases
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Indexed keywords
ASPARAGINE;
ASPARTIC ACIDS;
CATALYTIC MECHANISMS;
DFT;
XYLANASES;
AMINO ACIDS;
BACILLI;
BACTERIOLOGY;
ENERGY MANAGEMENT;
HYDROGEN;
HYDROGEN BONDS;
HYDROLYSIS;
ORGANIC ACIDS;
QUANTUM CHEMISTRY;
QUANTUM THEORY;
REACTION INTERMEDIATES;
SUGARS;
CATALYST ACTIVITY;
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EID: 79953685447
PISSN: 01413910
EISSN: None
Source Type: Journal
DOI: 10.1016/j.polymdegradstab.2011.01.010 Document Type: Article |
Times cited : (7)
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References (20)
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