Modifying the catalytic preference of tributyrin in Bacillus thermocatenulatus lipase through in-silico modeling of enzyme-substrate complex

Protein Engineering, Design and Selection

Volumn 26, Issue 5, 2013, Pages 325-333

  Durmaz, Emel ^a   Kuyucak, Serdar ^b   Sezerman, Ugur O ^a  

^a SABANCI UNIVERSITY   (Turkey)

^b UNIVERSITY OF SYDNEY   (Australia)

Author keywords

enzyme kinetics; lipase; protein engineering; steered molecular dynamics

Indexed keywords

BINDING FREE ENERGY; ENZYME-SUBSTRATE COMPLEXES; HETEROLOGOUS PROTEINS; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; STEERED MOLECULAR DYNAMICS; TRANSITION STATE COMPLEX;

BACTERIOLOGY; BINDING ENERGY; BIOCHEMICAL ENGINEERING; ENZYME KINETICS; GENETIC ENGINEERING; HYDROLYSIS; MOLECULAR DYNAMICS; SUBSTRATES;

LIPASES;

TRIACYLGLYCEROL LIPASE; TRIBUTYRIN; TRIOCTANOIN;

ARTICLE; BACILLUS; BACILLUS THERMOCATENULATUS; COMPUTER MODEL; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; STEADY STATE; WILD TYPE;

BACILLUS; CAPRYLATES; LIPASE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; THERMODYNAMICS; TRIGLYCERIDES;

GEOBACILLUS THERMOCATENULATUS;

EID: 84876551490     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzt004     Document Type: Article

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