Pyranose oxidase

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pyranose oxidase
1tt0.jpg
Pyranose oxidase tetramer, Trametes ochracea
Identifiers
EC no.1.1.3.10
CAS no.37250-80-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction

D-glucose + O2 2-dehydro-D-glucose + H2O2

Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are 2-dehydro-D-glucose and H2O2.

Pyranose oxidase is able to oxidize D-xylose, L-sorbose, D-galactose,[1] and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.[2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyranose:oxygen 2-oxidoreductase. Other names in common use include glucose 2-oxidase, and pyranose-2-oxidase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.

Structural studies[edit]

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1TT0, 1TZL, 2F5V, 2F6C, 2IGK, 2IGM, 2IGN, and 2IGO.

Use in biosensors[edit]

Recently, pyranose oxidase has been gaining on popularity within biosensors.[1] Unlike glucose oxidase, it can produce higher power output, given that it is not glycosylated, has more favorable value of Michaelis-Menten constants, and can catalytically convert both anomers of glucose. It reacts with a wider range of substrates. Pyranose oxidase does not cause an unwanted pH shift. It is also possible to easily express and produce it in high yields using E. coli.[1]

References[edit]

  1. ^ a b c Abrera AT, Sützl L, Haltrich D (April 2020). "Pyranose oxidase: A versatile sugar oxidoreductase for bioelectrochemical applications". Bioelectrochemistry. 132: 107409. doi:10.1016/j.bioelechem.2019.107409. PMID 31821902.
  2. ^ Janssen FW, Ruelius HW (November 1968). "Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II. Specificity and characterization of reaction products". Biochimica et Biophysica Acta. 167 (3): 501–10. doi:10.1016/0005-2744(68)90040-5. PMID 5722278.

Further reading[edit]