Highly selective bile acid hydroxylation by the multifunctional bacterial P450 monooxygenase CYP107D1 (OleP)

Objective Regio- and stereoselective hydroxylation of lithocholic acid (LCA) using CYP107D1 (OleP), a cytochrome P450 monooxygenase from the oleandomycin synthesis pathway of Streptomyces antibioticus . Results Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/Pd...

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Veröffentlicht in:Biotechnology letters 2020-05, Vol.42 (5), p.819-824
Hauptverfasser: Grobe, Sascha, Wszołek, Agata, Brundiek, Henrike, Fekete, Melinda, Bornscheuer, Uwe T.
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container_end_page 824
container_issue 5
container_start_page 819
container_title Biotechnology letters
container_volume 42
creator Grobe, Sascha
Wszołek, Agata
Brundiek, Henrike
Fekete, Melinda
Bornscheuer, Uwe T.
description Objective Regio- and stereoselective hydroxylation of lithocholic acid (LCA) using CYP107D1 (OleP), a cytochrome P450 monooxygenase from the oleandomycin synthesis pathway of Streptomyces antibioticus . Results Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/PdX from Pseudomonas putida was performed in Escherichia coli whole cells. In vivo hydroxylation of LCA exclusively yielded the 6β-OH product murideoxycholic acid (MDCA). In resting cells, 19.5% of LCA was converted to MDCA within 24 h, resulting in a space time yield of 0.04 mmol L −1 h −1 . NMR spectroscopy confirmed the identity of MDCA as the sole product. Conclusions The multifunctional P450 monooxygenase CYP107D1 (OleP) can hydroxylate LCA, forming MDCA as the only product.
doi_str_mv 10.1007/s10529-020-02813-4
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Results Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/PdX from Pseudomonas putida was performed in Escherichia coli whole cells. In vivo hydroxylation of LCA exclusively yielded the 6β-OH product murideoxycholic acid (MDCA). In resting cells, 19.5% of LCA was converted to MDCA within 24 h, resulting in a space time yield of 0.04 mmol L −1 h −1 . NMR spectroscopy confirmed the identity of MDCA as the sole product. Conclusions The multifunctional P450 monooxygenase CYP107D1 (OleP) can hydroxylate LCA, forming MDCA as the only product.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-020-02813-4</identifier><identifier>PMID: 31974648</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Applied Microbiology ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bile ; bile acids ; Biocatalysis ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Cloning, Molecular ; cytochrome P-450 ; Cytochrome P-450 Enzyme System - genetics ; Cytochrome P-450 Enzyme System - metabolism ; Cytochrome P450 ; Cytochrome P450 monooxygenase ; Cytochromes P450 ; Deoxycholic Acid - metabolism ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - growth &amp; development ; Ferredoxin ; Hydroxylation ; Life Sciences ; Lithocholic Acid - chemistry ; Magnetic resonance spectroscopy ; Microbiology ; NMR ; NMR spectroscopy ; Nuclear magnetic resonance ; nuclear magnetic resonance spectroscopy ; Oleandomycin ; Original Research Paper ; Oxidoreductases - genetics ; Oxidoreductases - metabolism ; oxygenases ; Pseudomonas putida ; Pseudomonas putida - enzymology ; Pseudomonas putida - genetics ; Reductase ; Reductases ; Stereoselectivity ; Streptomyces antibioticus - enzymology ; Streptomyces antibioticus - genetics</subject><ispartof>Biotechnology letters, 2020-05, Vol.42 (5), p.819-824</ispartof><rights>The Author(s) 2020</rights><rights>Biotechnology Letters is a copyright of Springer, (2020). 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Results Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/PdX from Pseudomonas putida was performed in Escherichia coli whole cells. In vivo hydroxylation of LCA exclusively yielded the 6β-OH product murideoxycholic acid (MDCA). In resting cells, 19.5% of LCA was converted to MDCA within 24 h, resulting in a space time yield of 0.04 mmol L −1 h −1 . NMR spectroscopy confirmed the identity of MDCA as the sole product. 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Results Co-expression of CYP107D1 from S. antibioticus and the reductase/ferredoxin system PdR/PdX from Pseudomonas putida was performed in Escherichia coli whole cells. In vivo hydroxylation of LCA exclusively yielded the 6β-OH product murideoxycholic acid (MDCA). In resting cells, 19.5% of LCA was converted to MDCA within 24 h, resulting in a space time yield of 0.04 mmol L −1 h −1 . NMR spectroscopy confirmed the identity of MDCA as the sole product. Conclusions The multifunctional P450 monooxygenase CYP107D1 (OleP) can hydroxylate LCA, forming MDCA as the only product.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>31974648</pmid><doi>10.1007/s10529-020-02813-4</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-0685-2696</orcidid><oa>free_for_read</oa></addata></record>
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subjects Applied Microbiology
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bile
bile acids
Biocatalysis
Biochemistry
Biomedical and Life Sciences
Biotechnology
Cloning, Molecular
cytochrome P-450
Cytochrome P-450 Enzyme System - genetics
Cytochrome P-450 Enzyme System - metabolism
Cytochrome P450
Cytochrome P450 monooxygenase
Cytochromes P450
Deoxycholic Acid - metabolism
E coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - growth & development
Ferredoxin
Hydroxylation
Life Sciences
Lithocholic Acid - chemistry
Magnetic resonance spectroscopy
Microbiology
NMR
NMR spectroscopy
Nuclear magnetic resonance
nuclear magnetic resonance spectroscopy
Oleandomycin
Original Research Paper
Oxidoreductases - genetics
Oxidoreductases - metabolism
oxygenases
Pseudomonas putida
Pseudomonas putida - enzymology
Pseudomonas putida - genetics
Reductase
Reductases
Stereoselectivity
Streptomyces antibioticus - enzymology
Streptomyces antibioticus - genetics
title Highly selective bile acid hydroxylation by the multifunctional bacterial P450 monooxygenase CYP107D1 (OleP)
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