Bioinformatic analysis of alpha/beta-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities

Protein Engineering, Design and Selection

Volumn 25, Issue 11, 2012, Pages 689-697

  Suplatov, D A ^a   Besenmatter, W ^b   Svedas V K ^a   Svendsen, A ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b NOVOZYMES A S   (Denmark)

Author keywords

hydrolases; bioinformatic analysis; CALB; catalytic promiscuity; subfamily specific positions

Indexed keywords

ALPHA-BETA; AMIDASE; BIOINFORMATIC ANALYSIS; CALB; CANDIDA ANTARCTICA LIPASE B; CATALYTIC CONVERSION; CATALYTIC FUNCTIONS; CATALYTIC PROMISCUITY; ENZYME ENGINEERING; ENZYME-SUBSTRATE COMPLEXES; FUNCTIONAL DISCRIMINATION; IN-SILICO SCREENING; LIPASE ACTIVITY; STRUCTURAL FRAMEWORKS; STRUCTURE-FUNCTION RELATIONSHIP; SUBFAMILY-SPECIFIC POSITIONS;

AMIDES; CATALYSIS; CATALYST ACTIVITY; HYDROLASES; KNOWLEDGE BASED SYSTEMS; LIPASES; PROFESSIONAL ASPECTS; RATIONAL FUNCTIONS;

BIOINFORMATICS;

AMIDASE; LIPASE B; PEPTIDASE; TRIACYLGLYCEROL LIPASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; BIOINFORMATICS; CANDIDA ANTARCTICA; CATALYSIS; COMPUTER MODEL; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ENGINEERING; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR MODEL; MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION;

AMIDOHYDROLASES; AMINO ACID SUBSTITUTION; CANDIDA; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; FUNGAL PROTEINS; HUMANS; HYDROLASES; LIPASE; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

CANDIDA ANTARCTICA;

EID: 84868572912     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs068     Document Type: Conference Paper

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