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Literature summary extracted from

  • Moller, M.S.; Vester-Christensen, M.B.; Jensen, J.M.; Hachem, M.A.; Henriksen, A.; Svensson, B.
    Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors (2015), J. Biol. Chem., 290, 12614-12629.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.142 in complex with its endogenous inhibitor LDI, at 2.7 A resolution. A hydrophobic cluster flanked by ionic interactions in the protein-protein interface is vital for the picomolar affinity of LDI to the enzyme Hordeum vulgare

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.142 D730R modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI Hordeum vulgare
3.2.1.142 D730W modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.142 Hordeum vulgare O48541
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Synonyms

EC Number Synonyms Comment Organism
3.2.1.142 HvLD99
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 Hordeum vulgare