Deletion of a dynamic surface loop improves stability and changes kinetic behavior of phosphatidylinositol-synthesizing Streptomyces phospholipase D

Biotechnology and Bioengineering

Volumn 111, Issue 4, 2014, Pages 674-682

  Damnjanović, Jasmina ^a   Nakano, Hideo ^a   Iwasaki, Yugo ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

Flexible loops; Phospholipase D; Stability

Indexed keywords

CONVERGENCE OF NUMERICAL METHODS; MOLECULAR DYNAMICS; POLYOLS;

FLEXIBLE LOOPS; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D; STREPTOMYCES PHOSPHOLIPASE; TEMPERATURE-DEPENDENT SOLUBILITIES; THERMOSTABILIZATION; TRANSPHOSPHATIDYLATION;

BACTERIA;

INOSITOL; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D;

ARTICLE; CONTROLLED STUDY; DELETION MUTANT; ENZYME SYNTHESIS; HALF LIFE TIME; HEAT TOLERANCE; HIGH TEMPERATURE; KINETICS; MOLECULAR DYNAMICS; MUTAGENESIS; NONHUMAN; SOLUBILITY; STREPTOMYCES ANTIBIOTICUS; STRUCTURE ANALYSIS; THERMOSTABILITY;

ANIMALIA; BACTERIA (MICROORGANISMS); STREPTOMYCES; STREPTOMYCES ANTIBIOTICUS;

FLEXIBLE LOOPS; PHOSPHOLIPASE D; STABILITY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ENZYME STABILITY; HOT TEMPERATURE; KINETICS; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLINOSITOLS; PHOSPHOLIPASE D; PLIABILITY; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE DELETION; STREPTOMYCES;

EID: 84894231107     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25149     Document Type: Article

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