Barley α-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the β→α loop 2 of the catalytic (β/α)8-barrel and is critical for activity and substrate specificity

European Journal of Biochemistry

Volumn 269, Issue 22, 2002, Pages 5377-5390

  Mori, Haruhide ^a,b   Bak Jensen, Kristian Sass ^a   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Binding subsite engineering; Glycoside hydrolase family 13; Oligosaccharide hydrolysis; Plant amylases; Site directed mutagenesis

Indexed keywords

2 CHLORO 4 NITROPHENYL BETA DEXTRO MALTOHEPTAOSIDE; 4 NITROPHENYL ALPHA DEXTRO MALTOHEXAOSIDE; AMYLASE; AMYLOSE; CARBOHYDRATE DERIVATIVE; GLYCOSIDASE; METHIONINE; UNCLASSIFIED DRUG;

ARTICLE; BARLEY; BINDING AFFINITY; BINDING SITE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; GLYCOSYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN POLYMERIZATION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ACARBOSE; ALPHA-AMYLASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ESCHERICHIA COLI; GLYCOSYLATION; HORDEUM; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; ISOELECTRIC FOCUSING; KINETICS; METHIONINE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TIME FACTORS;

EMBRYOPHYTA; HORDEUM VULGARE SUBSP. VULGARE;

EID: 0036439021     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03185.x     Document Type: Article

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