The N-terminal region of the starch-branching enzyme from Phaseolus vulgaris L. is essential for optimal catalysis and structural stability

Phytochemistry

Volumn 68, Issue 10, 2007, Pages 1367-1375

  Hamada, Shigeki ^a   Ito, Hiroyuki ^a   Ueno, Hiroshi ^a   Takeda, Yasuhito ^b   Matsui, Hirokazu ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

Chimeric enzyme; Kidney bean; Kinetics; Leguminosae; Phaseolus vulgaris L.; Site directed mutagenesis; Starch branching enzyme

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; HYBRID PROTEIN; ISOENZYME; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BEAN; CATALYSIS; CHEMICAL MODEL; CHEMISTRY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

1,4-ALPHA-GLUCAN BRANCHING ENZYME; AMINO ACID SEQUENCE; CATALYSIS; ISOENZYMES; KINETICS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHASEOLUS; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP;

FABACEAE; PHASEOLUS VULGARIS;

EID: 34247529977     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2007.02.024     Document Type: Article

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