Pentalenene oxygenase

Pentalenene oxygenase
Identifiers
EC no.1.14.15.32
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

Pentalenene oxygenase (EC 1.14.15.32, formerly EC 1.14.13.133, PtlI) is an enzyme with systematic name pentalenene,NADPH:oxygen 13-oxidoreductase.[1] This enzyme is involved in the biosyntheses of pentalenolactone and other antibiotics.[2] Additionally, it catalyses the following overall chemical reactions:

2D representation of the chemical structure of Q27102286.
pentalenene
+ 4 reduced
ferredoxin
 
 
2 O2
3 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27132511.
pentalen-13-al
+ 4 oxidised
ferredoxin
 
2D representation of the chemical structure of Q27132511.
pentalen-13-al
 
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27137207.
1-deoxypentalenic-acid

Pentalenene oxygenase from Streptomyces avermitilis is an oxidoreductase which uses molecular oxygen to insert a hydroxy group into 1-deoxypentalenic acid.[2] It requires ferredoxin to transfer electrons to the cytochrome P450 active site.[3]

Structure of pentalenolactone

The starting material is made as part of the biosynthetic pathway to pentalenolactone.[4]

References

  1. ↑ Quaderer R, Omura S, Ikeda H, Cane DE (October 2006). "Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis". Journal of the American Chemical Society. 128 (40): 13036–7. Bibcode:2006JAChS.12813036Q. doi:10.1021/ja0639214. PMC 2533730. PMID 17017767.
  2. 1 2 Li, Jing; Zhang, Chengde; Wu, Shiwen; Xue, Jiao; Chen, Ke; Deng, Zixin; Zhu, Dongqing (2025-06-01). "Cytochrome P450-catalyzed allylic oxidation of pentalenene to 1-deoxypentalenic acid in pentalenolactone biosynthesis". Engineering Microbiology. 5 (2) 100206. doi:10.1016/j.engmic.2025.100206. ISSN 2667-3703.
  3. ↑ Enzyme 1.14.15.32 at KEGG Pathway Database.
  4. ↑ You Z, Omura S, Ikeda H, Cane DE (March 2007). "Pentalenolactone biosynthesis: Molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate". Archives of Biochemistry and Biophysics. 459 (2): 233–40. doi:10.1016/j.abb.2006.11.016. PMC 1857356. PMID 17178094.
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