3.2.1.142: limit dextrinase
This is an abbreviated version!
For detailed information about limit dextrinase, go to the full flat file.
Word Map on EC 3.2.1.142
-
3.2.1.142
-
barley
-
malt
-
pullulan
-
amylopectin
-
isoamylase
-
diastatic
-
3.2.1.41
-
pullulanases
-
analysis
-
starch-branching
-
beta-limit
-
food industry
-
beta-amylase
-
synthesis
-
brewing
- 3.2.1.142
- barley
- malt
- pullulan
- amylopectin
- isoamylase
-
diastatic
-
3.2.1.41
- pullulanases
- analysis
-
starch-branching
-
beta-limit
- food industry
- beta-amylase
- synthesis
- brewing
Reaction
Synonyms
Ask, GH13 12-14, HvLD99, limit dextrinase, Pul3YH5, PULI, pullulanase, pullulanase type I, starch-debranching enzyme
ECTree
3.2.1.142 limit dextrinaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.142 - limit dextrinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A885S
single nucleotide polymorphism associated with thermostability
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
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
L102R/T233A/S235G/G298A/C415R/A885S/G888C
amino acid substitutions identified by alignment of the limit dextrinase sequences of varieties Galleon and Maud
T233A
single nucleotide polymorphism associated with thermostability
additional information
additional information
EPZ37738
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
additional information
-
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
-
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
