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Literature summary for 1.1.3.4 extracted from

  • Bright, H.J.; Porter, D.J.T.
    Flavoprotein oxidases (1975), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 12, 421-505.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Br- competitive, at low pH Aspergillus niger
Br- competitive, at low pH Penicillium amagasakiense
Cl- competitive, at low pH Aspergillus niger
Cl- competitive, at low pH Penicillium amagasakiense
F- competitive, at low pH Aspergillus niger
F- competitive, at low pH Penicillium amagasakiense

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
160000
-
-
Aspergillus niger
160000
-
-
Penicillium amagasakiense
186000
-
-
Aspergillus niger

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-glucose + O2 + H2O Aspergillus niger
-
D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 + H2O Penicillium amagasakiense
-
D-glucono-1,5-lactone + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Penicillium amagasakiense
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 + H2O
-
Penicillium amagasakiense D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 + H2O kinetic mechanism Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 + H2O kinetic mechanism Penicillium amagasakiense D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 + H2O glucose is the primary substrate for the enzyme Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

Subunits

Subunits Comment Organism
dimer
-
Aspergillus niger
dimer each unit in the dimer is composed of two polypeptide chains connected by a disulfide bond Penicillium amagasakiense

Cofactor

Cofactor Comment Organism Structure
FAD defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior Aspergillus niger
FAD defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior Penicillium amagasakiense