The 'pair of sugar tongs' site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity

FEBS Journal

Volumn 274, Issue 19, 2007, Pages 5055-5067

  Bozonnet, Sophie ^a,b   Jensen, Morten T ^b   Nielsen, Morten M ^a   Aghajari, Nushin ^c   Jensen, Malene H ^c   Kramhøft, Birte ^a,b   Willemoës, Martin ^a,b   Tranier, Samuel ^c   Haser, Richard ^c   Svensson, Birte ^a,b  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

^c UNIVERSITÉ DE LYON   (France)

Author keywords

Barley amylase; Crystal structures; Secondary carbohydrate binding sites; Starch granules; Surface plasmon resonance

Indexed keywords

ACARBOSE; ALPHA AMYLASE 1; ALPHA AMYLASE 2; AMYLASE; AMYLOSE; BETA CYCLODEXTRIN; MUTANT PROTEIN; OLIGOSACCHARIDE; PROLINE; SEPHAROSE; SUGAR; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BARLEY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PURIFICATION; ENZYME SYNTHESIS; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; SURFACE PLASMON RESONANCE; WILD TYPE;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; BASE SEQUENCE; BETA-CYCLODEXTRINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; HORDEUM; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; SURFACE PLASMON RESONANCE;

HORDEUM;

EID: 34748886064     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06024.x     Document Type: Article

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