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

BRENDA support

Literature summary for 1.1.3.4 extracted from

  • Kelley, R.L.; Reddy, C.A.
    Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium (1986), J. Bacteriol., 166, 269-274.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
CuCl2 stimulation of activity, 123% relative activity to no addition Phanerodontia chrysosporium
KCN stimulation of activity, 135% relative activity to no addition Phanerodontia chrysosporium
NaF weak stimulation of activity, 111% relative activity to no addition Phanerodontia chrysosporium

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 75% inhibition at 10 mM Phanerodontia chrysosporium
CN- not inhibitory Phanerodontia chrysosporium
CuSO4 not inhibitory Phanerodontia chrysosporium
F- not inhibitory Phanerodontia chrysosporium
o-phthalate 88% inhibition at 50 mM 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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
-
?
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

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
-
?
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 ?
-
?

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD 1.5 mol of flavin per mol of protein Phanerodontia chrysosporium