Literature summary for 3.2.1.3 extracted from

Surzhik, M.; Churkina, S.; Shmidt, A.; Shvetsov, A.; Kozhina, T.; Firsov, D.; Firsov, L.; Petukhov, M.
The effect of point amino acid substitutions in an internal alpha-helix on thermostability of Aspergillus awamori X100 glucoamylase (2010), Appl. Biochem. Microbiol., 46, 206-211.

Search for more literature for 3.2.1.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type enzyme in Saccharomyces cerevisiae strain C468, cloning and expression of mutant enzymes in Escherichia coli strain DH5alpha	Aspergillus awamori

Protein Variants

Protein Variants	Comment	Organism
A246C	site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect	Aspergillus awamori
G127A/P128A	site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein	Aspergillus awamori
G137A	site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect	Aspergillus awamori
G139A	site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect	Aspergillus awamori
I136L	site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect	Aspergillus awamori
additional information	molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview	Aspergillus awamori
P128A	site-directed mutagenesis, the mutant destabilizes the enzyme	Aspergillus awamori
P128A/G139A/I136L	site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A	Aspergillus awamori

Organism

Organism	UniProt	Comment	Textmining
Aspergillus awamori	-	-	-
Aspergillus awamori X100	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides	Aspergillus awamori	?	-	?
additional information	the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides	Aspergillus awamori X100	?	-	?

Synonyms

Synonyms	Comment	Organism
glucoamylase	-	Aspergillus awamori

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	-	assay at	Aspergillus awamori

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	assay at	Aspergillus awamori

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Release 2023.1 (January 2023)