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Literature summary for 1.1.3.4 extracted from

  • Witt, S.; Singh, M.; Kalisz, H.M.
    Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli (1998), Appl. Environ. Microbiol., 64, 1405-1411.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.4

Cloned(Commentary)

Cloned (Comment) Organism
cloning of the gene encoding the enzyme and expression in Escherichia coli Penicillium amagasakiense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.7
-
 beta-D-glucose native enzyme Penicillium amagasakiense
6.2
-
 beta-D-glucose recombinant enzyme Penicillium amagasakiense
6.3
-
 beta-D-glucose deglycosylated enzyme Penicillium amagasakiense
8.3
-
 2-deoxy-D-glucose recombinant enzyme Penicillium amagasakiense
106
-
 D-mannose recombinant enzyme Penicillium amagasakiense
384
-
 D-xylose recombinant enzyme Penicillium amagasakiense
952
-
 D-galactose recombinant enzyme Penicillium amagasakiense

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 2 * 60000, SDS-PAGE, recombinant enzyme Penicillium amagasakiense
120000
-
 recombinant enzyme, native PAGE Penicillium amagasakiense

Organism

Organism UniProt Comment Textmining
Penicillium amagasakiense
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein recombinant enzyme is nonglycosylated Penicillium amagasakiense

Purification (Commentary)

Purification (Comment) Organism
of the reactivated recombinant enzyme, using mild acidification and anion-exchange chromatography on Q-Sepharose Penicillium amagasakiense

Renatured (Commentary)

Renatured (Comment) Organism
refolding after treatment with 8 M urea and 30 mM dithiothreitol and subsequent dilution in a buffer containing reduced glutathione, FAD and glycerol Penicillium amagasakiense

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Penicillium amagasakiense

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-glucose + O2 + H2O recombinant enzyme Penicillium amagasakiense 2-deoxy-D-glucono-1,5-lactone + H2O2
-
 ?
beta-D-glucose + O2 + H2O glucose is the primary substrate, recombinant enzyme Penicillium amagasakiense D-glucono-1,5-lactone + H2O2
-
 ?
D-galactose + O2 + H2O recombinant enzyme Penicillium amagasakiense ? + H2O2
-
 ?
D-xylose + O2 + H2O recombinant enzyme Penicillium amagasakiense ?
-
 ?
mannose + O2 + H2O recombinant enzyme Penicillium amagasakiense ? + H2O2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 60000, SDS-PAGE, recombinant enzyme Penicillium amagasakiense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28 40 recombinant enzyme Penicillium amagasakiense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1950
-
 beta-D-glucose deglycosylated enzyme Penicillium amagasakiense
2000
-
 beta-D-glucose recombinant enzyme Penicillium amagasakiense
2000
-
 beta-D-glucose native enzyme Penicillium amagasakiense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2 6.2 recombinant enzyme Penicillium amagasakiense

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 5.2 recombinant enzyme, exhibits more than 80% of the maximum activity Penicillium amagasakiense
5 7 recombinant enzyme, more than 90% of the residual activity retained after 72 h incubation at room temperature Penicillium amagasakiense
6.2 6.5 recombinant enzyme, exhibits more than 80% of the maximum activity Penicillium amagasakiense
7
-
 above, the recombinant enzyme is slightly less stable than native and deglycosylated enzyme Penicillium amagasakiense