Literature summary for 3.2.1.3 extracted from

Latorre-Garcia, L.; Adam, A.C.; Manzanares, P.; Polaina, J.
Improving the amylolytic activity of Saccharomyces cerevisiae glucoamylase by the addition of a starch binding domain (2005), J. Biotechnol., 118, 167-176.

Search for more literature for 3.2.1.3

Application

Application	Comment	Organism
biotechnology	improvement of the yeast enzyme for starch degradation in biotechnological applications by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, chimeric enzyme in Saccharomyces cerevisiae strain Y428, overview	Saccharomyces cerevisiae 'var. diastaticus'

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the chimeric mutant enzyme in Saccharomyces cerevisiae strain Y428	Saccharomyces cerevisiae 'var. diastaticus'

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a mutant enzymes with improved catalytic activity with substrate starch by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, overview	Saccharomyces cerevisiae 'var. diastaticus'

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae 'var. diastaticus'	-	an amylolytic strain, gene STA1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
starch + H2O	the native enzyme shows low activity with raw starch due to a lack in starch binding domain	Saccharomyces cerevisiae 'var. diastaticus'	starch + beta-D-glucose	-	?

Synonyms

Synonyms	Comment	Organism
glucoamylase	-	Saccharomyces cerevisiae 'var. diastaticus'
Sta1p	-	Saccharomyces cerevisiae 'var. diastaticus'

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Release 2023.1 (January 2023)