Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 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

EC Number Protein Variants Comment Organism
3.2.1.3 A246C site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect Aspergillus awamori
3.2.1.3 G127A/P128A site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein Aspergillus awamori
3.2.1.3 G137A site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect Aspergillus awamori
3.2.1.3 G139A site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect Aspergillus awamori
3.2.1.3 I136L site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect Aspergillus awamori
3.2.1.3 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
3.2.1.3 P128A site-directed mutagenesis, the mutant destabilizes the enzyme Aspergillus awamori
3.2.1.3 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

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus awamori
-
-
-
3.2.1.3 Aspergillus awamori X100
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 glucoamylase
-
 Aspergillus awamori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 50
-
 assay at Aspergillus awamori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4.5
-
 assay at Aspergillus awamori