User:Jvonborstel9/Methylmalonyl-CoA
Evaluation:[edit]
Title is short and simple, gives the exact enzyme being discussed.
First sentence is clear and concise but could be "dumbed down" a little to make sense to the general public.
Lead section summarizes the barebones of what Methylmalonyl CoA is but does little to expand on it and give reasons that it is relevant.
There are no quotations or copied sources.
The subject is understandable from a general standpoint for the most part, but some terms (thioester, for example) are not of general knowledge and could be generalized.
Audience can interpret the information however they wish as the article is an unbiased reporting of facts.
The grammar and spelling are correct, sentences are complete, and there is no first or second person writing.
There are too many headings considering how few words are on the page, but this is mainly because very little is written about the subject.
There are only two sources. Both are legitimate but both are far too old to be relevant.
Most mentions of subjects found on Wikipedia are linked in the article.
Overall, there is nothing wrong with the article, it merely needs to be fleshed out a bit, with more details given. The sources used are also few and old, more newer sources should be researched and used. Pictures and diagrams would also benefit the article. Finally, some of the language needs to be generalize so that the average person could understand it. All in all, the main issue with the article is how little in contains in terms of overall information.
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Article Draft[edit]
Methylmalonyl-CoA[edit]
Methylmalonyl-CoA is the thioester consisting of coenzyme A linked to methylmalonic acid. It is an important intermediate in the biosynthesis of succinyl-CoA, which plays an essential role in the tricarboxylic acid cycle (aka the Citric Acid Cycle, or Krebs Cycle)[1]. The compound is sometimes referred to as "methylmalyl-CoA"[2].
Biosynthesis and Conversions[edit]
Methylmalonyl-CoA results from the metabolism of fatty acid with an odd number of carbons or from cholesterol side-chains, forming Propionyl-CoA.[4] Propionyl-CoA and bicarbonate are converted to Methylmalonyl-CoA by the enzyme propionyl-CoA Carboxylase[1]. It then is converted into succinyl-CoA by methylmalonyl-CoA mutase (MUT). This reaction is a reversable isomerization. In this way, the compound enters the Citric Acid Cycle. The following diagram demonstrates the aforementioned reaction:[2]
Propionyl CoA + Bicarbonate → Methylmalonyl CoA → Succinyl CoA
Vitamin B12[edit]
Vitamin B12 plays an integral role in this reaction. Coenzyme B12 (adenosyl-cobalamin) is an organometallic form of Vitamin B12 and serves as the cofactor of Methylmalonyl-CoA mutase, which is an essential enzyme in the human body.[5] The transformation of Methylmalonyl-CoA to Succinyl-CoA by this enzyme is a radical reaction.[5]
Related Diseases[edit]
Human Methylmalonic Acidemia (MMA)[edit]
This disease occurs when methylmalonyl-CoA mutase is unable to isomerize sufficient amounts of methylmalonyl-CoA into succinyl-CoA[6]. This causes a buildup of propionic and/or methylmalonic acid, which has effects on infants ranging from severe brain damage to death[4]. The disease is linked to Vitamin B12, which is the metabolic precursor to methylmalonyl-CoA mutase.[6][3]
References[edit]
- ^ a b Wongkittichote, Parith; Ah Mew, Nicholas; Chapman, Kimberly A. (2017-12). "Propionyl-CoA carboxylase – A review". Molecular Genetics and Metabolism. 122 (4): 145–152. doi:10.1016/j.ymgme.2017.10.002. PMC 5725275. PMID 29033250.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: PMC format (link) - ^ a b Nelson, David L.; Cox, Michael M. (2005). Principles of Biochemistry (4th ed.). New York: W. H. Freeman. ISBN 0-7167-4339-6.
- ^ a b Froese, D. Sean; Fowler, Brian; Baumgartner, Matthias R. (2019-07). "Vitamin B 12 , folate, and the methionine remethylation cycle—biochemistry, pathways, and regulation". Journal of Inherited Metabolic Disease. 42 (4): 673–685. doi:10.1002/jimd.12009. ISSN 0141-8955.
{{cite journal}}: Check date values in:|date=(help) - ^ a b Baumgartner, Matthias R; Hörster, Friederike; Dionisi-Vici, Carlo; Haliloglu, Goknur; Karall, Daniela; Chapman, Kimberly A; Huemer, Martina; Hochuli, Michel; Assoun, Murielle; Ballhausen, Diana; Burlina, Alberto (2014-12). "Proposed guidelines for the diagnosis and management of methylmalonic and propionic acidemia". Orphanet Journal of Rare Diseases. 9 (1): 130. doi:10.1186/s13023-014-0130-8. ISSN 1750-1172. PMC 4180313. PMID 25205257.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ a b c Kräutler, Bernhard (2012), Stanger, Olaf (ed.), "Biochemistry of B12-Cofactors in Human Metabolism", Water Soluble Vitamins, vol. 56, Dordrecht: Springer Netherlands, pp. 323–346, doi:10.1007/978-94-007-2199-9_17, ISBN 978-94-007-2198-2, retrieved 2021-11-01
- ^ a b Takahashi-Iñiguez, Tóshiko; García-Hernandez, Enrique; Arreguín-Espinosa, Roberto; Flores, María Elena (2012-06). "Role of vitamin B12 on methylmalonyl-CoA mutase activity". Journal of Zhejiang University SCIENCE B. 13 (6): 423–437. doi:10.1631/jzus.B1100329. ISSN 1673-1581. PMC 3370288. PMID 22661206.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: PMC format (link)