Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	2 proteins
Enzyme class ^help_outline	EC 1.14.19.8 pentalenolactone synthase

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Name ^help_outline pentalenolactone F Identifier CHEBI:70789 Charge -1 Formula C15H17O5 InChIKey^help_outline UUDKOVSZNMZKND-BDAURDKOSA-M SMILES^help_outline [H][C@@]12CC(C)(C)C[C@]11[C@@]([H])(COC(=O)[C@]11CO1)C(=C2)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline reduced [2Fe-2S]-[ferredoxin] Identifier RHEA-COMP:10001 Reactive part ^help_outline
- Name ^help_outline [2Fe-2S]¹⁺ Identifier CHEBI:33738 Charge 1 Formula Fe2S2 InChIKey^help_outline MAGIRAZQQVQNKP-UHFFFAOYSA-N SMILES^help_outline S1[Fe]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 180 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline O₂ Identifier CHEBI:15379 (CAS: 7782-44-7) ^help_outline Charge 0 Formula O2 InChIKey^help_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILES^help_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,727 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline pentalenolactone Identifier CHEBI:70790 Charge -1 Formula C15H15O5 InChIKey^help_outline NUPNVWUYFVEAIT-UJJBCWTCSA-M SMILES^help_outline [H][C@@]12COC(=O)[C@]3(CO3)[C@@]11C=C(C)[C@@H](C)[C@@]1([H])C=C2C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline oxidized [2Fe-2S]-[ferredoxin] Identifier RHEA-COMP:10000 Reactive part ^help_outline
- Name ^help_outline [2Fe-2S]²⁺ Identifier CHEBI:33737 Charge 2 Formula Fe2S2 InChIKey^help_outline XSOVBBGAMBLACL-UHFFFAOYSA-N SMILES^help_outline S1[Fe+]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 180 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:34575	RHEA:34576	RHEA:34577	RHEA:34578
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	2 proteins
EC numbers ^help_outline	1.14.19.8
KEGG ^help_outline				R10162
MetaCyc ^help_outline		RXN-12653

Publications

Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone.

Zhu D., Seo M.J., Ikeda H., Cane D.E.

The penM and pntM genes from the pentalenolactone biosynthetic gene clusters of Streptomyces exfoliatus UC5319 and Streptomyces arenae TÜ469 were predicted to encode orthologous cytochrome P450s, CYP161C3 and CYP161C2, responsible for the final step in the biosynthesis of the sesquiterpenoid antib ... >> More

The penM and pntM genes from the pentalenolactone biosynthetic gene clusters of Streptomyces exfoliatus UC5319 and Streptomyces arenae TÜ469 were predicted to encode orthologous cytochrome P450s, CYP161C3 and CYP161C2, responsible for the final step in the biosynthesis of the sesquiterpenoid antibiotic pentalenolactone (1). Synthetic genes optimized for expression in Escherichia coli were used to obtain recombinant PenM and PntM, each carrying an N-terminal His(6)-tag. Both proteins showed typical reduced-CO UV maxima at 450 nm, and each bound the predicted substrate, pentalenolactone F (4), with K(D) values of 153 ± 14 and 126 ± 11 μM for PenM and PntM, respectively, as determined by UV shift titrations. PenM and PntM both catalyzed the oxidative rearrangement of 4 to 1 when incubated in the presence of NADPH, spinach ferredoxin, ferredoxin reductase, and O(2). The steady-state kinetic parameters were k(cat) = 10.5 ± 1.7 min(-1) and K(m) = 340 ± 100 μM 4 for PenM and k(cat) = 8.8 ± 0.9 min(-1) and K(m) = 430 ± 100 μM 4 for PntM. The in vivo function of both gene products was confirmed by the finding that the corresponding deletion mutants S. exfoliatus/ΔpenM ZD22 and S. arenae/ΔpntM ZD23 no longer produced pentalenolactone but accumulated the precursor pentalenolactone F. Complementation of each deletion mutant with either penM or pntM restored production of antibiotic 1. Pentalenolactone was also produced by an engineered strain of Streptomyces avermitilis that had been complemented with pntE, pntD, and either pntM or penM, as well as the S. avermitilis electron-transport genes for ferredoxin and ferrodoxin reductase, fdxD and fprD. << Less

J. Am. Chem. Soc. 133:2128-2131(2011) [PubMed] [EuropePMC]

RHEA:34575 pentalenolactone F + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = pentalenolactone + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 H2O

Enzymes

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Cross-references

Publications

Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone.