Talk:Nicotinamide cofactor analogues

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Wiki Education assignment: CHEM 378 - Biochemistry Lab

This article was the subject of a Wiki Education Foundation-supported course assignment, between 31 January 2022 and 22 May 2022. Further details are available on the course page. Student editor(s): Alexanderwaals (article contribs).

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Latest comment: 2 years ago1 comment1 person in discussion

It may be helpful to add a note on oxidoreductases given that is enzyme group the article topic would be involved in, explaining why nicotinamide is used as a cofactor

Stating the oxidized and reduced forms,those used in anabolic vs catabolic rxns may also be useful.

A note on why analogues are needed could also be added.

Proposed Addition Notes:

Background: Oxidoreducatses are enzymes that catalyze the transfer of a hydride ion between a substrate and a cofactor, in many cases, particularly those in metabolic reactions, that cofator is a form of nicotinamide adenine dinucleotide.^[1] Nicotinamide adenine dinucleotide phosphate (NADPH) is used in anabolic reactions while nicotinamide adenine dinucleotide (NAD+) is used in catabolic reactions.^[2]

Analogues: Unlike the human body, typical chemical reactions are unable to regenerate the cofactor for further use. Synthetic cofactors have been researched to solve this problem. The analogues have been synthesized from similar compounds such as 1,4-dihydronicotinamide. These synthetic cofactors have since been used to better understand the mechanisms of reactions especially when it comes to stereospecificty, which may be enhanced by metal ions. Analogues serve as an alternative to traditional regeneration techniques. ^[3] ^[4]

--Alexanderwaals (talk) 04:19, 3 May 2022 (UTC)Reply

References

^ https://doi.org/10.1016/j.bbapap.2017.11.005
^ dx.doi.org/10.1021/cs4011056
^ dx.doi.org/10.1021/cs4011056
^ doi.org/10.1002/anie.202017027

Add topic

[1] ttps://doi.org/10.1016/j.bbapap.2017.11.005

[2] x.doi.org/10.1021/cs4011056

[3] x.doi.org/10.1021/cs4011056

[4] .org/10.1002/anie.202017027

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