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Literature summary for 1.1.3.4 extracted from

  • Garzillo, A.M.V.; Di Paolo, S.; Fenice, M.; Petruccioli, M.; Buonocore, V.; Federici, F.
    Production, purification and characterization of glucose oxidase from Penicillium variabile P16 (1995), Biotechnol. Appl. Biochem., 22, 169-178.
No PubMed abstract available
Search for more literature for 1.1.3.4

Inhibitors

Inhibitors Comment Organism Structure
Ag+ inhibition is explained by the high reactivity of this ion for thiol groups essential for enzymic activity Talaromyces variabilis
AgNO3 24% activity remains at 10 mM Talaromyces variabilis
CuCl2 6.5% activity remains at 10 mM Talaromyces variabilis
NaF 72% activity remains at 10 mM Talaromyces variabilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6
-
 beta-D-glucose
-
 Talaromyces variabilis
20
-
 2-deoxy-D-glucose
-
 Talaromyces variabilis
33
-
 D-xylose
-
 Talaromyces variabilis
44
-
 D-mannose
-
 Talaromyces variabilis
117
-
 D-maltose
-
 Talaromyces variabilis
162
-
 D-fructose
-
 Talaromyces variabilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
 2 * 62000, SDS-PAGE Talaromyces variabilis
126000
-
 gel filtration Talaromyces variabilis

Organism

Organism UniProt Comment Textmining
Talaromyces variabilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using ion-exchange chromatography on DEAE-Sepharose and gel filtration chromatography on Sephacryl S-300 Talaromyces variabilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Talaromyces variabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-glucose + O2 + H2O 19.6% relative activity to D-glucose Talaromyces variabilis 2-deoxy-D-glucono-1,5-lactone + H2O2
-
 ?
beta-D-glucose + O2 + H2O highly specific Talaromyces variabilis D-glucono-1,5-lactone + H2O2
-
 ?
beta-D-glucose + O2 + H2O glucose is the primary substrate for the enzyme Talaromyces variabilis D-glucono-1,5-lactone + H2O2
-
 ?
D-fructose + O2 + H2O 4.9% relative activity to D-glucose Talaromyces variabilis ? + H2O2
-
 ?
D-maltose + O2 + H2O 21.3% relative activity to D-glucose Talaromyces variabilis ? + H2O2
-
 ?
D-xylose + O2 + H2O 3% relative activity to D-glucose Talaromyces variabilis ?
-
 ?
mannose + O2 + H2O 7.2% relative activity to D-glucose Talaromyces variabilis ? + H2O2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 62000, SDS-PAGE Talaromyces variabilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Talaromyces variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 completely inactive Talaromyces variabilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Talaromyces variabilis