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

BRENDA support

Literature summary for 3.2.1.3 extracted from

  • Wong, D.W.; Robertson, G.H.; Lee, C.C.; Wagschal, K.
    Synergistic action of recombinant alpha-amylase and glucoamylase on the hydrolysis of starch granules (2007), Protein J., 26, 159-164.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae using the yeast phosphoglycerate kinase gene promoter with the original vector signal sequence eliminated, co-expression with a barley alpha-amylase 1 mutant with constitutive secretion in active forms Lentinula edodes

Protein Variants

Protein Variants Comment Organism
additional information co-expressed recombinant barley alpha-amylase 1 mutant and recombinant GLA synergistically enhanced the rate of hydrolysis by about 3fold for corn and wheat starch granules, compared to the sum of the individual activities, exo-endo synergism, reaction ratios, overview Lentinula edodes

General Stability

General Stability Organism
the recombinant enzyme stability is enhanced by 27% by Ca2+ at 0.1 mM Lentinula edodes

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 53% inhibition at 10 mM Lentinula edodes
EDTA slight inhibition Lentinula edodes
Fe2+ 29% inhibition at 10 mM Lentinula edodes
Mg2+ slight inhibition Lentinula edodes

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ bound Ca2+ in the enzyme molecule is essential at 50°C Lentinula edodes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Lentinula edodes
-
D-glucose + ?
-
?

Organism

Organism UniProt Comment Textmining
Lentinula edodes
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O
-
Lentinula edodes D-glucose + ?
-
?
starch + H2O soluble corn and wheat starch granules Lentinula edodes D-glucose + ?
-
?

Synonyms

Synonyms Comment Organism
GLA
-
Lentinula edodes
glucoamylase
-
Lentinula edodes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Lentinula edodes

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50
-
Lentinula edodes

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
recombinant enzyme, stable up to, stability is enhanced by Ca2+ Lentinula edodes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6
-
-
Lentinula edodes