Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 9, 2012, Pages 1008-1012

  Mller, Marie Sofie ^a,b   Abou Hachem, Maher ^a   Svensson, Birte ^a   Henriksen, Anette ^b  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

Author keywords

1,6 glucoside debranching; barley limit dextrinase; glycoside hydrolase family 13

Indexed keywords

GLYCOSIDASE; PULLULANASE; STARCH;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; HORDEUM; METABOLISM; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY;

GLYCOSIDE HYDROLASES; HORDEUM; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; STARCH; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

HORDEUM;

EID: 84865724994     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112031004     Document Type: Article

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