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Volumn 61, Issue 3-4, 2009, Pages 162-167
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The effect of substitution of Phe181 and Phe182 with Ala on activity, substrate specificity and stabilization of substrate at the active site of Bacillus thermocatenulatus lipase
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Author keywords
Bacillus thermocatenulatus; Lid; Lipase; Site directed mutagenesis; Steric hindrance; van der Waals
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Indexed keywords
ACTIVE SITE;
ACYL CHAIN;
CIRCULAR DICHROISM;
CONSERVED RESIDUES;
EFFECT OF SUBSTITUTION;
ENZYME ACTIVE SITES;
LIPASE ACTIVITY;
PHENYL GROUP;
SECONDARY STRUCTURES;
SITE DIRECTED MUTAGENESIS;
STERIC HINDRANCES;
SUBSTRATE SPECIFICITY;
TRIACYLGLYCEROLS;
VAN DER WAALS;
VAN DER WAALS INTERACTIONS;
AMINO ACIDS;
BACTERIOLOGY;
CHEMICAL REACTIONS;
CIRCULAR DICHROISM SPECTROSCOPY;
DICHROISM;
FLUORINE CONTAINING POLYMERS;
GLYCEROL;
MUTAGENESIS;
SUBSTRATES;
VAN DER WAALS FORCES;
LIPASES;
ALANINE;
MUTANT PROTEIN;
PHENYL GROUP;
PHENYLALANINE 181;
PHENYLALANINE 182;
PHENYLALANINE DERIVATIVE;
SERINE;
TRIACYLGLYCEROL;
TRIACYLGLYCEROL LIPASE;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ARTICLE;
BACILLUS;
BACILLUS THERMOCATENULATUS;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME SPECIFICITY;
ENZYME STABILITY;
ENZYME SUBSTRATE;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PROTEIN INTERACTION;
PROTEIN SECONDARY STRUCTURE;
SITE DIRECTED MUTAGENESIS;
GEOBACILLUS THERMOCATENULATUS;
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EID: 72049106382
PISSN: 13811177
EISSN: None
Source Type: Journal
DOI: 10.1016/j.molcatb.2009.06.006 Document Type: Article |
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Times cited : (32)
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References (22)
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