Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability

Protein Engineering, Design and Selection

Volumn 21, Issue 12, 2008, Pages 737-744

  Kuwahara, K ^a   Angkawidjaja, C ^a   Matsumura, H ^a,b   Koga, Y ^a   Takano, K ^a,b   Kanaya, S ^a  

^a OSAKA UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Ca2+ binding site; Crystal structure; Family I.3 lipase; Pseudomonas sp. MIS38; Site directed mutagenesis

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CALCIUM; CRYSTAL STRUCTURE; POWDERS;

ACTIVE SITES; CA2+-BINDING SITE; CATALYTIC DOMAINS; ESTERASE ACTIVITIES; FAMILY I.3 LIPASE; MUTANT PROTEINS; OPEN CONFORMATIONS; PSEUDOMONAS SP.; PSEUDOMONAS SP. MIS38; SITE-DIRECTED MUTAGENESIS;

BINDING SITES;

ESTERASE; TRIACYLGLYCEROL LIPASE; CALCIUM; MUTANT PROTEIN;

ARTICLE; BINDING SITE; CALCIUM BINDING; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PSEUDOMONAS; X RAY DIFFRACTION; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STABILITY; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

PSEUDOMONAS SP.;

CALCIUM; CATALYTIC DOMAIN; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; LIPASE; MUTANT PROTEINS; MUTATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STABILITY; PSEUDOMONAS; TEMPERATURE;

EID: 56549095312     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn057     Document Type: Article

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