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Literature summary for 1.1.3.4 extracted from

  • Janati-Fard, F.; Housaindokht, M.; Monhemi, H.
    Investigation of structural stability and enzymatic activity of glucose oxidase and its subunits (2016), J. Mol. Catal. B, 134, 16-24 .
No PubMed abstract available
Search for more literature for 1.1.3.4

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 1GPE Penicillium amagasakiense

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Penicillium amagasakiense P81156
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2
-
 Penicillium amagasakiense D-glucono-1,5-lactone + H2O2
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 66700, SDS-PAGE and crystal structure analysis Penicillium amagasakiense
More enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis Penicillium amagasakiense

Synonyms

Synonyms Comment Organism
pen-GOx
-
 Penicillium amagasakiense

Cofactor

Cofactor Comment Organism Structure
FAD enzyme pen-GOx contains one mol of tightly but not covalently bound FAD cofactor at the active site of each subunit. The FAD-binding domain of GOx is formed by a beta-sheet lid. The lid prevents the release of FAD from the dimer. Loosening of tertiary structure leads to opening of this lid, causing FAD loss anddissociation of the dimer. Loss of FAD from GOx is concurrent with tertiary structure loss. FAD, especially isoalloxazine, is important for the catalytic activity for beta-D-glucose. The binding of FAD cofactor also plays a key role on the catalytic activity of flavoproteins for the correct folding, assembly and protein stability. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis Penicillium amagasakiense

General Information

General Information Comment Organism
additional information enzyme structure and structure-activity relationship analysis and molecular dynamic simulations, detailed overview. Active-site residues of pen-GOx are two histidines, His520 and His563, which act as general base and general acid in the reductive half-reaction and the oxidative half-reaction, respectively Penicillium amagasakiense