Widely Distributed Bifunctional Bacterial Cytochrome P450 Enzymes Catalyze both Intramolecular C−C Bond Formation in cyclo‐l‐Tyr‐l‐Tyr and Its Coupling with Nucleobases

Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1–gymA6 in Escherichia coli resulted in the formation of...

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Published in	Angewandte Chemie International Edition Vol. 61; no. 21; pp. e202200377 - n/a
Main Authors	Liu, Jing, Harken, Lauritz, Yang, Yiling, Xie, Xiulan, Li, Shu‐Ming
Format	Journal Article
Language	English
Published	WEINHEIM Wiley 16.05.2022 Wiley Subscription Services, Inc John Wiley and Sons Inc
Edition	International ed. in English
Subjects	Adducts Bases (nucleic acids) Biocatalysts Biosynthesis Biosynthetic Pathways Catalysis Chemistry Chemistry, Multidisciplinary Coupling Cyclodipeptide Synthase Cytochrome Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Cytochrome P450 Enzymes Cytochromes P450 E coli Enzymes Escherichia coli - genetics Escherichia coli - metabolism Gene clusters Guanine Hypoxanthine Natural Products Nucleobase Transferase Phylogeny Physical Sciences Science & Technology Transferases - metabolism Tryptophan Tyrosine Nucleobase Transferase Natural Products GENE-CLUSTER PATHWAY Cytochrome P450 Enzymes CYP121 Biosynthesis DIVERSITY IDENTIFICATION Cyclodipeptide Synthase
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Abstract	Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1–gymA6 in Escherichia coli resulted in the formation of cyclo‐l‐Tyr‐l‐Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1–GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C−C coupling within cyclo‐l‐Tyr‐l‐Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine‐containing guatyromycines, instead of the reported tryptophan‐nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Bioinformatic analysis unveiled a widely distributed two‐gene locus (gym) in actinobacteria. Reconstruction of the biosynthetic pathways and biochemical investigation led to the characterization of the cytochrome P450s GymBs as dual‐functional oxidases, which catalyze both intra‐ and intermolecular coupling reactions at different positions of cyclo‐l‐Tyr‐l‐Tyr to generate novel tyrosine‐based alkaloids.
AbstractList	Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA 1 – gymA 6 in Escherichia coli resulted in the formation of cyclo ‐ l ‐Tyr‐ l ‐Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB 1 –GymB 6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C−C coupling within cyclo ‐ l ‐Tyr‐ l ‐Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine‐containing guatyromycines, instead of the reported tryptophan‐nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1–gymA6 in Escherichia coli resulted in the formation of cyclo‐l‐Tyr‐l‐Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1–GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C−C coupling within cyclo‐l‐Tyr‐l‐Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine‐containing guatyromycines, instead of the reported tryptophan‐nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA -gymA in Escherichia coli resulted in the formation of cyclo-l-Tyr-l-Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB -GymB act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C-C coupling within cyclo-l-Tyr-l-Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine-containing guatyromycines, instead of the reported tryptophan-nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1–gymA6 in Escherichia coli resulted in the formation of cyclo‐l‐Tyr‐l‐Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1–GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C−C coupling within cyclo‐l‐Tyr‐l‐Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine‐containing guatyromycines, instead of the reported tryptophan‐nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Bioinformatic analysis unveiled a widely distributed two‐gene locus (gym) in actinobacteria. Reconstruction of the biosynthetic pathways and biochemical investigation led to the characterization of the cytochrome P450s GymBs as dual‐functional oxidases, which catalyze both intra‐ and intermolecular coupling reactions at different positions of cyclo‐l‐Tyr‐l‐Tyr to generate novel tyrosine‐based alkaloids. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA(1)-gymA(6) in Escherichia coli resulted in the formation of cyclo-l-Tyr-l-Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB(1)-GymB(6) act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C-C coupling within cyclo-l-Tyr-l-Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine-containing guatyromycines, instead of the reported tryptophan-nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1 -gymA6 in Escherichia coli resulted in the formation of cyclo-l-Tyr-l-Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1 -GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C-C coupling within cyclo-l-Tyr-l-Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine-containing guatyromycines, instead of the reported tryptophan-nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class.Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA1 -gymA6 in Escherichia coli resulted in the formation of cyclo-l-Tyr-l-Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB1 -GymB6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C-C coupling within cyclo-l-Tyr-l-Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine-containing guatyromycines, instead of the reported tryptophan-nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin and guatyromycine biosynthesis. Expression of the cyclodipeptide synthase genes gymA 1 – gymA 6 in Escherichia coli resulted in the formation of cyclo ‐ l ‐Tyr‐ l ‐Tyr as the major product. Reconstruction of the biosynthetic pathways in Streptomyces albus and biochemical investigation proved that the cytochrome P450 enzymes GymB 1 –GymB 6 act as both intramolecular oxidases and intermolecular nucleobase transferases. They catalyze not only the oxidative C−C coupling within cyclo ‐ l ‐Tyr‐ l ‐Tyr, leading to mycocyclosin, but also its connection with guanine and hypoxanthine, and are thus responsible for the formation of tyrosine‐containing guatyromycines, instead of the reported tryptophan‐nucleobase adducts. Phylogenetic data suggest the presence of at least 47 GymB orthologues, indicating the occurrence of a widely distributed enzyme class. Bioinformatic analysis unveiled a widely distributed two‐gene locus ( gym ) in actinobacteria. Reconstruction of the biosynthetic pathways and biochemical investigation led to the characterization of the cytochrome P450s GymBs as dual‐functional oxidases, which catalyze both intra‐ and intermolecular coupling reactions at different positions of cyclo ‐ l ‐Tyr‐ l ‐Tyr to generate novel tyrosine‐based alkaloids.
ArticleNumber	202200377
Author	Li, Shu‐Ming Harken, Lauritz Liu, Jing Yang, Yiling Xie, Xiulan
AuthorAffiliation	2 Fachbereich Chemie Philipps-Universität Marburg Hans-Meerwein-Straße 4 35032 Marburg Germany 1 Institut für Pharmazeutische Biologie und Biotechnologie Fachbereich Pharmazie Philipps-Universität Marburg Robert-Koch-Straße 4 35037 Marburg Germany
AuthorAffiliation_xml	– name: 1 Institut für Pharmazeutische Biologie und Biotechnologie Fachbereich Pharmazie Philipps-Universität Marburg Robert-Koch-Straße 4 35037 Marburg Germany – name: 2 Fachbereich Chemie Philipps-Universität Marburg Hans-Meerwein-Straße 4 35032 Marburg Germany
Author_xml	– sequence: 1 givenname: Jing surname: Liu fullname: Liu, Jing organization: Philipps-Universität Marburg – sequence: 2 givenname: Lauritz surname: Harken fullname: Harken, Lauritz organization: Philipps-Universität Marburg – sequence: 3 givenname: Yiling surname: Yang fullname: Yang, Yiling organization: Philipps-Universität Marburg – sequence: 4 givenname: Xiulan surname: Xie fullname: Xie, Xiulan organization: Philipps-Universität Marburg – sequence: 5 givenname: Shu‐Ming orcidid: 0000-0003-4583-2655 surname: Li fullname: Li, Shu‐Ming email: shuming.li@staff.uni-marburg.de organization: Philipps-Universität Marburg
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Keywords	Nucleobase Transferase Natural Products GENE-CLUSTER PATHWAY Cytochrome P450 Enzymes CYP121 Biosynthesis DIVERSITY IDENTIFICATION Cyclodipeptide Synthase
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SSID	ssj0028806
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Snippet	Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two‐gene clusters for mycocyclosin... Tailoring enzymes are important modification biocatalysts in natural product biosynthesis. We report herein six orthologous two-gene clusters for mycocyclosin...
Source	Web of Science
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StartPage	e202200377
SubjectTerms	Adducts Bases (nucleic acids) Biocatalysts Biosynthesis Biosynthetic Pathways Catalysis Chemistry Chemistry, Multidisciplinary Coupling Cyclodipeptide Synthase Cytochrome Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Cytochrome P450 Enzymes Cytochromes P450 E coli Enzymes Escherichia coli - genetics Escherichia coli - metabolism Gene clusters Guanine Hypoxanthine Natural Products Nucleobase Transferase Phylogeny Physical Sciences Science & Technology Transferases - metabolism Tryptophan Tyrosine
Title	Widely Distributed Bifunctional Bacterial Cytochrome P450 Enzymes Catalyze both Intramolecular C−C Bond Formation in cyclo‐l‐Tyr‐l‐Tyr and Its Coupling with Nucleobases
URI	https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.202200377 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000772002400001 https://www.ncbi.nlm.nih.gov/pubmed/35201649 https://www.proquest.com/docview/2660943775 https://www.proquest.com/docview/2632802249 https://pubmed.ncbi.nlm.nih.gov/PMC9401060
Volume	61
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