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Literature summary for 3.2.1.3 extracted from

  • Xian, L.; Feng, J.X.
    Purification and biochemical characterization of a novel mesophilic glucoamylase from Aspergillus tritici WZ99 (2018), Int. J. Biol. Macromol., 107, 1122-1130 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information EDTA and Na2EDTA do not affect the enzyme activity Aspergillus tritici

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons Aspergillus tritici

Inhibitors

Inhibitors Comment Organism Structure
Fe2+ activates at 1-5 mM, inhibits at 10 mM Aspergillus tritici
Fe3+ activates at 1-5 mM, inhibits at 10 mM Aspergillus tritici
additional information EDTA and Na2EDTA do not affect the enzyme activity Aspergillus tritici

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C Aspergillus tritici

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aspergillus tritici
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates at 1-10 mM Aspergillus tritici
Fe2+ activates at 1-5 mM, inhibits at 10 mM Aspergillus tritici
Fe3+ activates at 1-5 mM, inhibits at 10 mM Aspergillus tritici
Mn2+ activates at 1-10 mM Aspergillus tritici

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Aspergillus tritici
-
?
-
?
starch + H2O Aspergillus tritici CGMCC 3.15694.3.2
-
?
-
?
starch + H2O Aspergillus tritici WZ99
-
?
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus tritici A0A1S6XZP1 isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
-
Aspergillus tritici CGMCC 3.15694.3.2 A0A1S6XZP1 isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
-
Aspergillus tritici WZ99 A0A1S6XZP1 isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme 53.64fold by ammonium sulfate fractionation, hydrophobic interaction chromatography, ion exchange chromatography, and native PAGE Aspergillus tritici

Reaction

Reaction Comment Organism Reaction ID
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages Aspergillus tritici

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
18.73
-
substrate pullalan, pH 5.0, 45°C Aspergillus tritici
30.14
-
substrate soluble potato starch, pH 5.0, 45°C Aspergillus tritici
34.3
-
substrate amylose, pH 5.0, 45°C Aspergillus tritici
36.73
-
substrate amylopectin, pH 5.0, 45°C Aspergillus tritici
39.64
-
substrate soluble wheat starch, pH 5.0, 45°C Aspergillus tritici

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O
-
Aspergillus tritici ?
-
?
amylose + H2O
-
Aspergillus tritici ?
-
?
amylose + H2O
-
Aspergillus tritici CGMCC 3.15694.3.2 ?
-
?
amylose + H2O
-
Aspergillus tritici WZ99 ?
-
?
additional information the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages Aspergillus tritici ?
-
?
additional information the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages Aspergillus tritici CGMCC 3.15694.3.2 ?
-
?
additional information the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages Aspergillus tritici WZ99 ?
-
?
pullulan + H2O low activity Aspergillus tritici ?
-
?
pullulan + H2O low activity Aspergillus tritici CGMCC 3.15694.3.2 ?
-
?
pullulan + H2O low activity Aspergillus tritici WZ99 ?
-
?
starch + H2O
-
Aspergillus tritici ?
-
?
starch + H2O standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch Aspergillus tritici ?
-
?
starch + H2O
-
Aspergillus tritici CGMCC 3.15694.3.2 ?
-
?
starch + H2O standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch Aspergillus tritici CGMCC 3.15694.3.2 ?
-
?
starch + H2O
-
Aspergillus tritici WZ99 ?
-
?
starch + H2O standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch Aspergillus tritici WZ99 ?
-
?

Subunits

Subunits Comment Organism
? x * 51000, extracellular enzyme, SDS-PAGE Aspergillus tritici

Synonyms

Synonyms Comment Organism
AtriGA15A
-
Aspergillus tritici
glucoamylase
-
Aspergillus tritici

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Aspergillus tritici

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 55 over 50% of maximal activity at 30-55°C Aspergillus tritici

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
purified extracellular enzyme, pH 5.0, 1 h, stable up to Aspergillus tritici
50
-
purified extracellular enzyme, pH 5.0, 1 h, loss of 50% activity Aspergillus tritici
60
-
purified extracellular enzyme, pH 5.0, 1 h, inactivation Aspergillus tritici

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
67.15
-
starch pH 5.0, 45°C Aspergillus tritici

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5 5
-
Aspergillus tritici

pH Range

pH Minimum pH Maximum Comment Organism
3.5 10.5 85% of maximal activity at pH 4.0-10.0, and 70% of maximal activity at pH 3.5 and 75% at pH 10.5, respectively Aspergillus tritici

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 10 purified extracellular enzyme, 4°C, stable at Aspergillus tritici

General Information

General Information Comment Organism
evolution the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15 Aspergillus tritici

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
additional information Kcat/Km value is calculated as 4.47 l/g/s Aspergillus tritici