N'-Formylkynurenine
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| Systematic IUPAC name
(2S)-2-Amino-4-(2-formamidophenyl)-4-oxobutanoic acid | |
| Other names
N′-Formyl-L-kynurenine
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| Identifiers | |
3D model (JSmol)
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| KEGG | |
| MeSH | N'-formylkynurenine |
PubChem CID
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| Properties | |
| C11H12N2O4 | |
| Molar mass | 236.227 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references
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N′-Formylkynurenine is an intermediate in the catabolism of tryptophan. It is a formylated derivative of kynurenine. The formation of N′-formylkynurenine is catalyzed by heme dioxygenases.[1]
Biosynthesis
The enzyme indoleamine 2,3-dioxygenase is the first and rate-limiting enzyme of tryptophan catabolism through the kynurenine pathway.[2]
Related enzymes performing a similar function are Indoleamine 2,3-dioxygenase 2 and tryptophan 2,3-dioxygenase.[3][4]
Metabolism
In the main sequence of the kynurenine pathway, the formyl group is removed by the enzyme arylformamidase, giving the compound after which the pathway is named:[5]
Alternatively, the enzyme kynureninase can produce N-formylanthranilic acid and L-alanine:[6][7]
References
- ^ Basran, Jaswir; Efimov, Igor; Chauhan, Nishma; Thackray, Sarah J; Krupa, James L; Eaton, Graham; Griffith, Gerry A; Mowat, Christopher G; Handa, Sandeep; Raven, Emma Lloyd (2011). "The Mechanism of Formation of N-Formylkynurenine by Heme Dioxygenases". Journal of the American Chemical Society. 133 (40): 16251–16257. Bibcode:2011JAChS.13316251B. doi:10.1021/ja207066z. PMC 3210546. PMID 21892828.
- ^ Yamazaki, F.; Kuroiwa, T.; Takikawa, O.; Kido, R. (1985). "Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme". Biochemical Journal. 230 (3): 635–638. doi:10.1042/bj2300635. PMC 1152665. PMID 3877502.
- ^ Yuasa, Hajime J.; Mizuno, Keiko; Ball, Helen J. (2015). "Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable". The FEBS Journal. 282 (14): 2735–2745. doi:10.1111/febs.13316. PMID 25950090.
- ^ Pilotte, Luc; Larrieu, Pierre; Stroobant, Vincent; Colau, Didier; Dolušić, Eduard; Frédérick, Raphaël; De Plaen, Etienne; Uyttenhove, Catherine; Wouters, Johan; Masereel, Bernard; Van Den Eynde, Benoît J. (2012). "Reversal of tumoral immune resistance by inhibition of tryptophan 2,3-dioxygenase". Proceedings of the National Academy of Sciences. 109 (7): 2497–2502. doi:10.1073/pnas.1113873109. PMC 3289319. PMID 22308364.
- ^ Jakoby, William B. (1954). "Kynurenine Formamidase from Neurospora". Journal of Biological Chemistry. 207 (2): 657–663. doi:10.1016/S0021-9258(18)65682-0. PMID 13163050.
- ^ Alberati-Giani, Dsniela; Buchli, Rico; Malherbe, Pari; Broger, Clemens; Lang, Gabrielle; Köhler, Christer; Lahm, Hans-Werner; Cesura, Andrea M. (1996). "Isolation and Expression of a cDNA Clone Encoding Human Kynureninase". European Journal of Biochemistry. 239 (2): 460–468. doi:10.1111/j.1432-1033.1996.0460u.x. PMID 8706755.
- ^ Enzyme 3.7.1.3 at KEGG Pathway Database.