Literature summary for 1.1.3.5 extracted from

  • Fapyane, D.; Poulsen, C.; Ferapontova, E.
    Bioelectrocatalytic oxidation of glucose by hexose oxidase directly wired to graphite (2016), Electrochem. Commun., 65, 1-4 .
No PubMed abstract available

Application

Application Comment Organism
additional information the enzyme is a good candidate for bioelectrochemical applications. Electrochemical study of electron transfer reactions and bioelectrocatalysis of glucose oxidation by enzyme HOX immobilized on graphite electrodes Chondrus crispus

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Hansenula polymorpha, i.e. Ogataea angusta Chondrus crispus

Engineering

Protein Variants Comment Organism
additional information the purified enzyme HOX is immobilized on graphite electrodes. In the case of direct electronic wiring of HOX, O2 no longer acts as an electron acceptor, and it is the electrode that operates as an electron sink, which may affect the biocatalytic activity of enzymes due to the changed environment/conformation in the active site in the absence of a natural small molecular substrate. The formal potential of FAD in HOX estimated as a mean value of the anodic and cathodic peak potentials is less negative than that of free FAD adsorbed directly onto graphite electrodes Chondrus crispus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7
-
D-glucose pH 7.0, temperature not specified in the publication Chondrus crispus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
126000
-
-
Chondrus crispus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Chondrus crispus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Hox
-
Chondrus crispus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8 6.3
-
Chondrus crispus

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme possesses a single catalytic FAD center covalently bound through His 79 and Cys 138 residues with improved stability and cofactor integrity. The redox transformation of FAD during biocatalysis involves a 2e?/2H+ transfer reaction, which is essential for enzymatic activities of FAD-containing enzymes. The formal potential of FAD in HOX, immobilized onto graphite electrodes, estimated as a mean value of the anodic and cathodic peak potentials is less negative than that of free FAD adsorbed directly onto graphite electrodes. Consistent with that, in the presence of glucose, bioelectrocatalysis of glucose oxidation by HOX starts from potentials exceeding those of HOX's FAD Chondrus crispus