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Literature summary for 3.2.1.3 extracted from

  • Marin-Navarro, J.; Gurgu, L.; Alamar, S.; Polaina, J.
    Structural and functional analysis of hybrid enzymes generated by domain shuffling between Saccharomyces cerevisiae (var. diastaticus) Sta1 glucoamylase and Saccharomycopsis fibuligera Bgl1 beta-glucosidase (2011), Appl. Microbiol. Biotechnol., 89, 121-130.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
var. diastaticus
-
Saccharomyces cerevisiae BY4741
-
var. diastaticus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
soluble starch + H2O
-
Saccharomyces cerevisiae ?
-
?
soluble starch + H2O
-
Saccharomyces cerevisiae BY4741 ?
-
?

Subunits

Subunits Comment Organism
More glucoamylase is a two-domain protein composed by a N-terminal serine–threonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
glucoamylase
-
Saccharomyces cerevisiae
Sta1
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium Saccharomyces cerevisiae