Improved activity and modulated action pattern obtained by random mutagenesis at the fourth β-α loop involved in substrate binding to the catalytic (β/β)8-barrel domain of barley α-amylase 1

Journal of Biological Chemistry

Volumn 272, Issue 36, 1997, Pages 22456-22463

  Matsui, Ikuo ^a,b   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b NATL INST BIOSCI HUM TECHNOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

ALPHA-AMYLASE; BLOTTING, WESTERN; CALCIUM CHLORIDE; CATALYSIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HORDEUM; ISOENZYMES; MUTAGENESIS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

HORDEUM VULGARE SUBSP. VULGARE;

EID: 0030883742     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.36.22456     Document Type: Article

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