Hydroperoxide lyase
In today's article, we will explore Hydroperoxide lyase and its impact on today's world in detail. From its origin to its evolution today, Hydroperoxide lyase has played a crucial role in different aspects of daily life. Over the years, Hydroperoxide lyase has sparked great interest and debate, generating multiple perspectives and opinions that have shaped its meaning and relevance in society. From his impact on popular culture to his influence on technology and science, Hydroperoxide lyase has left an indelible mark on the contemporary landscape. In this article, we will explore how Hydroperoxide lyase has shaped the world we live in and what its implications are for the future.
| Hydroperoxide lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.99.- | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Hydroperoxide lyases are enzymes that catalyze the cleavage of C-C bonds in the hydroperoxides of fatty acids. They belong to the cytochrome P450 enzyme family (CYP74C and CYP74B).[1]
Polyunsaturated fatty acids such as linolenic and linoleic acids are susceptible to formation of hydroperoxides upon contact with oxygen in air. Hydroperoxides are highly reactive functional groups since they contain an oxidant (O-O bond) adjacent to a reductant (C-H bonds). When flanked by olefins, the hydroperoxides can be induced to rearrange to give the hemiacetal. It is this reaction that is catalyzed by hydroperoxide lyases. The resulting aldehydes are notable as fragrances, green leaf volatiles, and antifeedants.[2]
References
- ^ Grechkin AN, Brühlmann F, Mukhtarova LS, Gogolev YV, Hamberg M (2006). "Hydroperoxide lyases (CYP74C and CYP74B) catalyze the homolytic isomerization of fatty acid hydroperoxides into hemiacetals". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1761 (12): 1419–28. doi:10.1016/j.bbalip.2006.09.002. PMID 17049304.
- ^ Matsui K (2006). "Green leaf volatiles: hydroperoxide lyase pathway of oxylipin metabolism". Current Opinion in Plant Biology. 9 (3): 274–80. doi:10.1016/j.pbi.2006.03.002. PMID 16595187.
Further reading
- Noordermeer MA, Veldink GA, Vliegenthart JF (2001). "Fatty acid hydroperoxide lyase: a plant cytochrome p450 enzyme involved in wound healing and pest resistance". ChemBioChem. 2 (7–8): 494–504. doi:10.1002/1439-7633(20010803)2:7/8<494::AID-CBIC494>3.0.CO;2-1. hdl:1874/5345. PMID 11828481. S2CID 29327220.
- Grechkin AN (2002). "Hydroperoxide lyase and divinyl ether synthase". Prostaglandins & Other Lipid Mediators. 68–69: 457–70. doi:10.1016/S0090-6980(02)00048-5. PMID 12432936.
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |