Insights into the role of the (α + β) insertion in the TIM-barrel catalytic domain, regarding the stability and the enzymatic activity of Chitinase A from Serratia marcescens

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 1, 2009, Pages 23-31

  Zees, Athanassios C ^a   Pyrpassopoulos, Serapion ^b,c   Vorgias, Constantinos E ^a  

^a UNIVERSITY OF ATHENS   (Greece)

^b INSTITUTE OF NANOSCIENCE AND NANOTECHNOLOGY   (Greece)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Chitinase; Enzyme engineering; Protein modelling; Serratia; Thermodynamics; TIM barrel insertion

Indexed keywords

CHITINASE; CHITINASE A; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; GENE DELETION; GENE INSERTION; GENETIC ENGINEERING; MOLECULAR BIOLOGY; NONHUMAN; PH; PRIORITY JOURNAL; SERRATIA MARCESCENS; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CHITINASE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SERRATIA MARCESCENS; SPECTRUM ANALYSIS; TEMPERATURE;

SERRATIA; SERRATIA MARCESCENS;

EID: 56449096137     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.09.018     Document Type: Article

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