Histidine 210 mutant of a trypsin-type Achromobacter protease I shows broad optimum pH range

Journal of Bioscience and Bioengineering

Volumn 93, Issue 3, 2002, Pages 331-333

  Shiraki, Kentaro ^a   Sakiyama, Fumio ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Catalytic triad; Optimum pH shift; pH dependence; Serine protease; Site directed mutagenesis

Indexed keywords

BIOELECTRIC PHENOMENA; CATALYSIS; CATALYST ACTIVITY; ENZYMES;

ELECTROSTATIC INTERACTIONS;

BIOCHEMISTRY;

BACTERIAL ENZYME; BRINASE;

ACHROMOBACTER; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; ELECTRICITY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; GENE MUTATION; NONHUMAN; PH;

ACHROMOBACTER; BACTERIA (MICROORGANISMS); BOVINAE; NEGIBACTERIA;

EID: 0036098708     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(02)80038-X     Document Type: Article

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