Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors

Journal of Biological Chemistry

Volumn 290, Issue 20, 2015, Pages 12614-12629

  Møller, Marie S ^a,b   Vester Christensen, Malene B ^a,b,c   Jensen, Johanne M ^a,b,d   Hachem, Maher Abou ^a   Henriksen, Anette ^b   Svensson, Birte ^a  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

^c NOVO NORDISK A S   (Denmark)

^d NOVOZYMES A S   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYMES; HYDROLASES; STARCH; SURFACE PLASMON RESONANCE;

ACTIVE SITE ARCHITECTURE; ENDOGENOUS INHIBITOR; HYDROPHOBIC CLUSTERS; MOLECULAR UNDERSTANDING; PHYLOGENETIC ANALYSIS; PROTEIN-PROTEIN INTERFACE; SITE DIRECTED MUTAGENESIS; STARCH DEBRANCHING ENZYMES;

CRYSTAL STRUCTURE;

GLYCOSIDASE INHIBITOR; OLIGO 1,6 GLUCOSIDASE; OLIGO 1,6 GLUCOSIDASE INHIBITOR; UNCLASSIFIED DRUG; ENZYME INHIBITOR; GLYCOSIDASE; PULLULANASE; STARCH; VEGETABLE PROTEIN;

ARTICLE; BARLEY; CEREAL; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SPECIFICITY; GERMINATION; HYDROPHOBICITY; MONOCOT; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; SURFACE PLASMON RESONANCE; ANTAGONISTS AND INHIBITORS; CHEMISTRY; ENZYMOLOGY; GENETICS; HORDEUM; METABOLISM; PHYSIOLOGY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

HORDEUM;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GERMINATION; GLYCOSIDE HYDROLASES; HORDEUM; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; STARCH; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84929347435     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.642777     Document Type: Article

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