Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 2,713 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cyclooctat-9-en-7-ol Identifier CHEBI:78352 Charge 0 Formula C20H34O InChIKeyhelp_outline JEGYHIKVYHOKQY-PNDCXJIESA-N SMILEShelp_outline [H][C@@]1(C)CC[C@]2([H])[C@]1([H])C[C@@]1(C)CC[C@H](C(C)C)\C1=C\C[C@]2(C)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 2,783 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cyclooctat-9-ene-5,7-diol Identifier CHEBI:141020 Charge 0 Formula C20H34O2 InChIKeyhelp_outline PAGWWOOUBKDVRF-NNLKJMRESA-N SMILEShelp_outline [H][C@@]1(C)C[C@@H](O)[C@]2([H])[C@]1([H])C[C@@]1(C)CC[C@H](C(C)C)\C1=C\C[C@]2(C)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56820 | RHEA:56821 | RHEA:56822 | RHEA:56823 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification, characterization and molecular adaptation of class I redox systems for the production of hydroxylated diterpenoids.
Goerner C., Schrepfer P., Redai V., Wallrapp F., Loll B., Eisenreich W., Haslbeck M., Brueck T.
<h4>Background</h4>De novo production of multi-hydroxylated diterpenoids is challenging due to the lack of efficient redox systems.<h4>Results</h4>In this study a new reductase/ferredoxin system from Streptomyces afghaniensis (AfR·Afx) was identified, which allowed the Escherichia coli-based produ ... >> More
<h4>Background</h4>De novo production of multi-hydroxylated diterpenoids is challenging due to the lack of efficient redox systems.<h4>Results</h4>In this study a new reductase/ferredoxin system from Streptomyces afghaniensis (AfR·Afx) was identified, which allowed the Escherichia coli-based production of the trihydroxylated diterpene cyclooctatin, a potent inhibitor of human lysophospholipase. This production system provides a 43-fold increase in cyclooctatin yield (15 mg/L) compared to the native producer. AfR·Afx is superior in activating the cylcooctatin-specific class I P450s CotB3/CotB4 compared to the conventional Pseudomonas putida derived PdR·Pdx model. To enhance the activity of the PdR·Pdx system, the molecular basis for these activity differences, was examined by molecular engineering.<h4>Conclusion</h4>We demonstrate that redox system engineering can boost and harmonize the catalytic efficiency of class I hydroxylase enzyme cascades. Enhancing CotB3/CotB4 activities also provided for identification of CotB3 substrate promiscuity and sinularcasbane D production, a functionalized diterpenoid originally isolated from the soft coral Sinularia sp. << Less
Microb. Cell Fact. 15:86-86(2016) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Cloning and heterologous expression of the cyclooctatin biosynthetic gene cluster afford a diterpene cyclase and two p450 hydroxylases.
Kim S.Y., Zhao P., Igarashi M., Sawa R., Tomita T., Nishiyama M., Kuzuyama T.
Cyclooctatin, a diterpene characterized by a 5-8-5 fused ring system, is a potent inhibitor of lysophospholipase. Here we report the cloning and characterization of a complete cyclooctatin biosynthetic gene cluster from Streptomyces melanosporofaciens MI614-43F2 and heterologous production of cycl ... >> More
Cyclooctatin, a diterpene characterized by a 5-8-5 fused ring system, is a potent inhibitor of lysophospholipase. Here we report the cloning and characterization of a complete cyclooctatin biosynthetic gene cluster from Streptomyces melanosporofaciens MI614-43F2 and heterologous production of cyclooctatin in S. albus. Sequence analysis coupled with subcloning and gene deletion revealed that the minimal cyclooctatin biosynthetic gene cluster consists of four genes, cotB1 to cotB4, encoding geranylgeranyl diphosphate (GGDP) synthase, terpene cyclase (CotB2), and two cytochromes P450, respectively. Incubation of the recombinant CotB2 with GGDP resulted in the formation of cyclooctat-9-en-7-ol, an unprecedented tricyclic diterpene alcohol. The present study establishes the complete biosynthetic pathway of cyclooctatin and provides insights into both the stereospecific diterpene cyclization mechanism of the GGDP cyclase and the molecular bases for the stereospecific and regiospecific hydroxylation. << Less
Chem. Biol. 16:736-743(2009) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.