Enzyme that oxidizes glucose to gluconic acid, with the formation of hydrogen peroxide. Used for specific quantitative determination of glucose, including urinary glucose excreted in diabetes, and also to remove traces of glucose from foodstuffs (e.g. from dried egg to prevent the Maillard reaction during storage). Originally isolated from the mould Penicillium notatum and called notatin.
Glucose oxidase
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n
An antibacterial flavoprotein enzyme obtained from Penicillium notatum and other fungi. It is antibacterial in the presence of glucose and oxygen.
| Wikipedia: Glucose oxidase |
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| PDB Molecule of the Month pdb77_1 | |||||||
| Identifiers | |||||||
| EC number | 1.1.3.4 | ||||||
| CAS number | 9001-37-0 | ||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB | structures | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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The glucose oxidase enzyme (GOx) (EC 1.1.3.4) binds to beta-D-glucopyranose (a hemiacetal form of the six-carbon sugar glucose) and aids in breaking the sugar down into its metabolites. GOx is a dimeric protein that catalyzes the oxidation of beta-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes to gluconic acid.
In order to work as a catalyst, GOx requires a cofactor, flavin adenine dinucleotide (FAD). FAD is a common component in biological oxidation-reduction (redox reactions). Redox reactions involve a gain or loss of electrons from a molecule. In the GOx-catalyzed redox reaction, FAD works as the initial electron acceptor and is reduced to FADH2. Then FADH2 is oxidized by the final electron acceptor, molecular oxygen (O2), which can do so because it has a higher reduction potential. O2 is then reduced to hydrogen peroxide (H2O2).
The glucose oxidase enzyme is commonly used in biosensors to detect levels of glucose by keeping track of the number of electrons passed through the enzyme by connecting it to an electrode and measuring the resulting charge. When produced commercially for this application, it is often extracted from Aspergillus niger. This has a possible application in the world of nanotechnology when used in conjunction with tiny electrodes as glucose sensors for diabetics.
Glucose oxidase is found in honey and acts as a natural preservative. GOx at the surface of the honey reduces atmospheric O2 to hydrogen peroxide (H2O2), which acts as an antimicrobial barrier.
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Notation and other names
Notation, extracted from antibacterial cultures of Penicillium notatum, was originally named Penicillin A, but was renamed to avoid confusion with penicillin.[1] Notatin was shown to be identical to Penicillin B and glucose oxidase, enzymes extracted from other molds besides P. notatum;[2] it is now generally known as glucose oxidase.[3]
Early experiments showed that notatin exhibits in vitro antibacterial activity (in the presence of glucose) due to hydrogen peroxide formation.[4][1] In vivo tests showed that notatin was not effective in protecting rodents from Streptococcus haemolyticus, Staphylococcus aureus, or salmonella, and caused severe tissue damage at some doses.[4]
See also
References
- ^ a b Coulthard CE, Michaelis R, Short WF, Sykes G (1945). "Notatin: an anti-bacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov". Biochem. J. 39 (1): 24–36. PMID 16747849.
- ^ KEILIN D, HARTREE EF (January 1952). "Specificity of glucose oxidase (notatin)". Biochem. J. 50 (3): 331–41. PMID 14915954.
- ^ Julio Raba and Horacio A. Mottola (1995). "Glucose Oxidase as an Analytical Reagent". Critical Reviews in Analytical Chemistry 25 (1): 1–42. http://www.biosensing.net/EBLA/Corso/Lezione%2001/GOD.PDF.
- ^ a b Broom WA, Coulthard CE, Gurd MR, Sharpe ME (December 1946). "Some pharmacological and chemotherapeutic properties of notatin". Br J Pharmacol Chemother 1 (4): 225–233. PMID 19108091.
External links
- "Glucose Oxidase: A much used and much loved enzyme in biosensors" at University of Paisley
- MeSH Glucose+Oxidase
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