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Literature summary for 1.1.3.4 extracted from

  • Kelley, R.L.; Reddy, C.A.
    Glucose oxidase of Phanerochaete chrysosporium (1988), Methods Enzymol., 161, 307-316.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
Phanerodontia chrysosporium
CN- not inhibitory Phanerodontia chrysosporium
CuSO4 not inhibitory Phanerodontia chrysosporium
F- not inhibitory Phanerodontia chrysosporium
o-phthalate
-
Phanerodontia chrysosporium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.95
-
O2
-
Phanerodontia chrysosporium
37 38 beta-D-glucose
-
Phanerodontia chrysosporium
38
-
beta-D-glucose
-
Phanerodontia chrysosporium
55.5
-
D-maltose
-
Phanerodontia chrysosporium
105.2
-
D-xylose
-
Phanerodontia chrysosporium
217.4
-
L-sorbose
-
Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information peroxisome-like structure Phanerodontia chrysosporium
-
-
periplasmic space
-
Phanerodontia chrysosporium 42597
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
2 * 80000, identical, SDS-PAGE Phanerodontia chrysosporium
175000 180000 gel filtration Phanerodontia chrysosporium
180000
-
gel filtration, overestimation may be due to hydrodynamic properties of the enzyme Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-glucose + O2 + H2O Phanerodontia chrysosporium
-
D-glucono-1,5-lactone + H2O2 in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid ?
additional information Phanerodontia chrysosporium the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin ?
-
?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
Phanerodontia chrysosporium

Purification (Commentary)

Purification (Comment) Organism
using column chromatography on DEAE-Sephadex, Sephacryl S-300 and DEAE-Sepharose Phanerodontia chrysosporium

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
Phanerodontia chrysosporium
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
15.1
-
oxidation of o-dianisidine at 37°C and pH 4.5 Phanerodontia chrysosporium

Storage Stability

Storage Stability Organism
frozen, at least 1 week Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
-
Phanerodontia chrysosporium D-glucono-1,5-lactone + H2O2 in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid ?
beta-D-glucose + O2 + H2O glucose is the primary substrate for the enzyme Phanerodontia chrysosporium D-glucono-1,5-lactone + H2O2
-
?
D-maltose + O2 + H2O 4.5% of D-glucose reactivity Phanerodontia chrysosporium ?
-
?
D-xylose + O2 + H2O 4.8% of D-glucose reactivity Phanerodontia chrysosporium ?
-
?
L-sorbose + O2 + H2O 5.8% of D-glucose reactivity Phanerodontia chrysosporium ?
-
?
additional information the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin Phanerodontia chrysosporium ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 80000, identical, SDS-PAGE Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6 5
-
Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
FAD 2 mol per mol of enzyme Phanerodontia chrysosporium