Literature summary for 3.2.1.142 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.

Search for more literature for 3.2.1.142

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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
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

Organism	UniProt	Comment	Textmining
Hordeum vulgare	O48541	-	-

Synonyms

Synonyms	Comment	Organism
HvLD99	-	Hordeum vulgare

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)