Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase

European Journal of Biochemistry

Volumn 271, Issue 2, 2004, Pages 253-262

  Synstad, Bjørnar ^a   Gåseidnes, Sigrid ^a   Van Aalten, Daan M F ^b   Vriend, Gert ^c   Nielsen, Jens E ^d,e   Eijsink, Vincent G H ^a  

^a NORWEGIAN UNIVERSITY OF LIFE SCIENCES   (Norway)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

^c RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Electrostatics; Mutagenesis; pH optimum; pKa; Serratia marcescens

Indexed keywords

ASPARTIC ACID; CHITINASE; ENZYME VARIANT; GLUTAMIC ACID; GLYCOSIDE; HYDROXYL GROUP; SERINE; SUGAR; TYROSINE;

ARTICLE; CATALYSIS; CATALYST; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME RELEASE; ENZYME SUBSTRATE; MATHEMATICAL COMPUTING; MUTATIONAL ANALYSIS; PH; PRIORITY JOURNAL; SERRATIA MARCESCENS;

ASPARTIC ACID; BINDING SITES; CATALYTIC DOMAIN; CHITINASE; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; CONSERVED SEQUENCE; DNA MUTATIONAL ANALYSIS; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; MUTATION; SERRATIA MARCESCENS; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

SERRATIA MARCESCENS;

EID: 1642521614     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03923.x     Document Type: Article

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