User:Justme26/L-gulonolactone oxidase
This is the sandbox page where you will draft your initial Wikipedia contribution.
If you're starting a new article, you can develop it here until it's ready to go live. If you're working on improvements to an existing article, copy only one section at a time of the article to this sandbox to work on, and be sure to use an edit summary linking to the article you copied from. Do not copy over the entire article. You can find additional instructions here. Remember to save your work regularly using the "Publish page" button. (It just means 'save'; it will still be in the sandbox.) You can add bold formatting to your additions to differentiate them from existing content. |
Article Draft
[edit]Lead
[edit]L-Gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C. Its expressed in mice and rats, but is non-functional in Haplorrhini (a suborder of primates, including humans), in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action.The structure of L-gulonolactone oxidase in rats helps identify characteristics of this enzyme.
Article body
[edit]L-gulonolactone oxidase in Rats
[edit]L-gulonolactone oxidase (GULO) is an enzyme that helps catalyze the production of ascorbic acid aka vitamin C. Mammals such as humans and guinea pigs do not express this gene due to multiple mutations in a specific exon.[1] These mutations correlate to nucleotide substitution.[2] Rats are a species that do express L-gulonolactone oxidase with a specific gene transcript. The protein coding region of the gene 645 base-pairs long, with eight exons and seven introns.[1] The amino acid sequence of this protein has suggested that rat L-Gulonolactone oxidase is located in the membrane portion of the endoplasmic reticulum due to its multiple B-sheet structure which contains hydrophobic areas.[3] It has been determined that rat GULO has a prosthetic domain in the N-terminus, flavian adenine dinucleotide. The only substrates that can make this rat enzyme function are L-GalL and L-GulL.[3]
References
- ^ a b ashpublications.org. doi:10.1182/blood.2019004158. PMC 7498365. PMID 32730592 https://ashpublications.org/blood/article/136/12/1394/461619/TET-family-dioxygenases-and-the-TET-activator. Retrieved 2024-05-03.
{{cite web}}
: Missing or empty|title=
(help)CS1 maint: PMC format (link) - ^ Aboobucker, Siddique I.; Lorence, Argelia (2016-01-01). "Recent progress on the characterization of aldonolactone oxidoreductases". Plant Physiology and Biochemistry. 98: 171–185. doi:10.1016/j.plaphy.2015.11.017. ISSN 0981-9428. PMC 4725720. PMID 26696130.
{{cite journal}}
: CS1 maint: PMC format (link) - ^ a b Paciolla, Costantino; Fortunato, Stefania; Dipierro, Nunzio; Paradiso, Annalisa; De Leonardis, Silvana; Mastropasqua, Linda; de Pinto, Maria Concetta (2019-11). "Vitamin C in Plants: From Functions to Biofortification". Antioxidants. 8 (11): 519. doi:10.3390/antiox8110519. ISSN 2076-3921. PMC 6912510. PMID 31671820.
{{cite journal}}
: Check date values in:|date=
(help)CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)