Marneral synthase
Marneral synthase (EC 5.4.99.53) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, marneral-forming).[1] This enzyme catalyses the following chemical reaction
- (3S)-2,3-epoxy-2,3-dihydrosqualene marneral
| Marneral synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.4.99.53 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Marneral is a triterpenoid formed by Grob fragmentation of the A ring of 2,3-epoxy-2,3-dihydrosqualene during cyclization. This aldehyde gains its name from its structural similarity to a class triterpenes commonly found in members of the Iridaceae, originally identified by Dr. Franz-Josef Marner[1]
This enzyme is a member of a metabolic gene cluster along with two other cytochrome P450s.[2]
References
- Xiong Q, Wilson WK, Matsuda SP (February 2006). "An Arabidopsis oxidosqualene cyclase catalyzes iridal skeleton formation by Grob fragmentation". Angewandte Chemie. 45 (8): 1285–8. doi:10.1002/anie.200503420. PMID 16425307.
- Field B, Fiston-Lavier AS, Kemen A, Geisler K, Quesneville H, Osbourn AE (September 2011). "Formation of plant metabolic gene clusters within dynamic chromosomal regions". Proceedings of the National Academy of Sciences of the United States of America. 108 (38): 16116–21. doi:10.1073/pnas.1109273108. PMC 3179108. PMID 21876149.
External links
- Marneral+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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