LIVIVO - Search results -

Search results

Result 1 - 10 of total 11

Search options

Article: Ribosome-independent peptide biosynthesis: the challenge of a unifying nomenclature

Dell, Maria / Dunbar, Kyle L. / Hertweck, Christian

Natural product reports. 2022 Mar. 23, v. 39, no. 3

2022

Abstract: The first machineries for non-ribosomal peptide (NRP) biosynthesis were uncovered over 50 years ago, and the dissection of these megasynthetases set the stage for the nomenclature system that has been used ever since. Although the number of exceptions to ...

Abstract	The first machineries for non-ribosomal peptide (NRP) biosynthesis were uncovered over 50 years ago, and the dissection of these megasynthetases set the stage for the nomenclature system that has been used ever since. Although the number of exceptions to the canonical biosynthetic pathways has surged in the intervening years, the NRP synthetase (NRPS) classification system has remained relatively unchanged. This has led to the exclusion of many biosynthetic pathways whose biosynthetic machineries violate the classical rules for NRP assembly, and ultimately to a rupture in the field of NRP biosynthesis. In an attempt to unify the classification of NRP pathways and to facilitate the communication within the research field, we propose a revised framework for grouping ribosome-independent peptide biosynthetic pathways based on recognizable commonalities in their biosynthetic logic. Importantly, the framework can be further refined as needed.
Keywords	biosynthesis ; dissection ; nonribosomal peptides
Language	English
Dates of publication	2022-0323
Size	p. 453-459.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/d1np00019e
Database	NAL-Catalogue (AGRICOLA)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Ribosome-independent peptide biosynthesis: the challenge of a unifying nomenclature.

Dell, Maria / Dunbar, Kyle L / Hertweck, Christian

Natural product reports

2022 Volume 39, Issue 3, Page(s) 453–459

Abstract	The first machineries for non-ribosomal peptide (NRP) biosynthesis were uncovered over 50 years ago, and the dissection of these megasynthetases set the stage for the nomenclature system that has been used ever since. Although the number of exceptions to the canonical biosynthetic pathways has surged in the intervening years, the NRP synthetase (NRPS) classification system has remained relatively unchanged. This has led to the exclusion of many biosynthetic pathways whose biosynthetic machineries violate the classical rules for NRP assembly, and ultimately to a rupture in the field of NRP biosynthesis. In an attempt to unify the classification of NRP pathways and to facilitate the communication within the research field, we propose a revised framework for grouping ribosome-independent peptide biosynthetic pathways based on recognizable commonalities in their biosynthetic logic. Importantly, the framework can be further refined as needed.
MeSH term(s)	Biosynthetic Pathways ; Peptide Biosynthesis, Nucleic Acid-Independent ; Peptide Synthases/metabolism ; Peptides/metabolism ; Ribosomes/metabolism
Chemical Substances	Peptides ; Peptide Synthases (EC 6.3.2.-)
Language	English
Publishing date	2022-03-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/d1np00019e
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Trapping of a Polyketide Synthase Module after C-C Bond Formation Reveals Transient Acyl Carrier Domain Interactions.

Dell, Maria / Tran, Mai Anh / Capper, Michael J / Sundaram, Srividhya / Fiedler, Jonas / Koehnke, Jesko / Hellmich, Ute A / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2024 Volume 63, Issue 9, Page(s) e202315850

Abstract: Modular polyketide synthases (PKSs) are giant assembly lines that produce an impressive range of biologically active compounds. However, our understanding of the structural dynamics of these megasynthases, specifically the delivery of acyl carrier ... ...

Abstract	Modular polyketide synthases (PKSs) are giant assembly lines that produce an impressive range of biologically active compounds. However, our understanding of the structural dynamics of these megasynthases, specifically the delivery of acyl carrier protein (ACP)-bound building blocks to the catalytic site of the ketosynthase (KS) domain, remains severely limited. Using a multipronged structural approach, we report details of the inter-domain interactions after C-C bond formation in a chain-branching module of the rhizoxin PKS. Mechanism-based crosslinking of an engineered module was achieved using a synthetic substrate surrogate that serves as a Michael acceptor. The crosslinked protein allowed us to identify an asymmetric state of the dimeric protein complex upon C-C bond formation by cryo-electron microscopy (cryo-EM). The possible existence of two ACP binding sites, one of them a potential "parking position" for substrate loading, was also indicated by AlphaFold2 predictions. NMR spectroscopy showed that a transient complex is formed in solution, independent of the linker domains, and photochemical crosslinking/mass spectrometry of the standalone domains allowed us to pinpoint the interdomain interaction sites. The structural insights into a branching PKS module arrested after C-C bond formation allows a better understanding of domain dynamics and provides valuable information for the rational design of modular assembly lines.
MeSH term(s)	Polyketide Synthases/metabolism ; Cryoelectron Microscopy ; Binding Sites ; Catalytic Domain ; Acyl Carrier Protein/metabolism
Chemical Substances	Polyketide Synthases (79956-01-7) ; Acyl Carrier Protein
Language	English
Publishing date	2024-01-17
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202315850
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Heterocomplex structure of a polyketide synthase component involved in modular backbone halogenation.

Fraley, Amy E / Dell, Maria / Schmalhofer, Maximilian / Meoded, Roy A / Bergande, Cedric / Groll, Michael / Piel, Jörn

Structure (London, England : 1993)

2023 Volume 31, Issue 5, Page(s) 565–572.e4

Abstract: Bacterial modular polyketide synthases (PKSs) generate diverse, complex and bioactive natural products that are constructed mainly based on principles of fatty acid biosynthesis. The cytotoxic oocydin-type polyketides contain a vinyl chloride moiety ... ...

Abstract	Bacterial modular polyketide synthases (PKSs) generate diverse, complex and bioactive natural products that are constructed mainly based on principles of fatty acid biosynthesis. The cytotoxic oocydin-type polyketides contain a vinyl chloride moiety introduced during polyketide chain elongation. Required for modular polyketide backbone halogenation are a non-heme iron and ɑ-ketoglutarate-dependent halogenase OocP and OocQ lacking characterized homologs. This work provides structural insights into these unusual PKS components and their interactions via a high-resolution X-ray crystallography structure of the heterocomplex. By mapping the protein-protein interactions and comparison with structures of similar halogenases, we illustrate the potential of this heterodimer complex as a replacement for the conserved homodimeric structure of homologous enzymes. The OocPQ protein pair has thus evolved as a means of stabilizing the halogenase and facilitating chemical transformations with great synthetic utility.
MeSH term(s)	Polyketide Synthases/genetics ; Polyketide Synthases/metabolism ; Halogenation ; Polyketides/metabolism ; Bacteria/metabolism
Chemical Substances	Polyketide Synthases (79956-01-7) ; Polyketides
Language	English
Publishing date	2023-03-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2023.02.010
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 4141: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Reconstitution of polythioamide antibiotic backbone formation reveals unusual thiotemplated assembly strategy.

Dunbar, Kyle L / Dell, Maria / Gude, Finn / Hertweck, Christian

Proceedings of the National Academy of Sciences of the United States of America

2020 Volume 117, Issue 16, Page(s) 8850–8858

Abstract: Closthioamide (CTA) is a rare example of a thioamide-containing nonribosomal peptide and is one of only a handful of secondary metabolites described from obligately anaerobic bacteria. Although the biosynthetic gene cluster responsible for CTA production ...

Abstract	Closthioamide (CTA) is a rare example of a thioamide-containing nonribosomal peptide and is one of only a handful of secondary metabolites described from obligately anaerobic bacteria. Although the biosynthetic gene cluster responsible for CTA production and the thioamide synthetase that catalyzes sulfur incorporation were recently discovered, the logic for peptide backbone assembly has remained a mystery. Here, through the use of in vitro biochemical assays, we demonstrate that the amide backbone of CTA is assembled in an unusual thiotemplated pathway involving the cooperation of a transacylating member of the papain-like cysteine protease family and an iteratively acting ATP-grasp protein. Using the ATP-grasp protein as a bioinformatic handle, we identified hundreds of such thiotemplated yet nonribosomal peptide synthetase (NRPS)-independent biosynthetic gene clusters across diverse bacterial phyla. The data presented herein not only clarify the pathway for the biosynthesis of CTA, but also provide a foundation for the discovery of additional secondary metabolites produced by noncanonical biosynthetic pathways.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Anti-Bacterial Agents/metabolism ; Bacteria, Anaerobic/enzymology ; Bacteria, Anaerobic/genetics ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Biosynthetic Pathways/genetics ; Computational Biology ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Genes, Bacterial ; Multigene Family ; Peptide Biosynthesis, Nucleic Acid-Independent/genetics ; Secondary Metabolism/genetics ; Thioamides/metabolism
Chemical Substances	Anti-Bacterial Agents ; Bacterial Proteins ; Thioamides ; closthioamide ; Adenosine Triphosphate (8L70Q75FXE) ; Cysteine Endopeptidases (EC 3.4.22.-)
Language	English
Publishing date	2020-04-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1918759117
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A Specialized Polythioamide-Binding Protein Confers Antibiotic Self-Resistance in Anaerobic Bacteria.

Gude, Finn / Molloy, Evelyn M / Horch, Therese / Dell, Maria / Dunbar, Kyle L / Krabbe, Jana / Groll, Michael / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2022 Volume 61, Issue 37, Page(s) e202206168

Abstract: Understanding antibiotic resistance mechanisms is central to the development of anti-infective therapies and genomics-based drug discovery. Yet, many knowledge gaps remain regarding the resistance strategies employed against novel types of antibiotics ... ...

Abstract	Understanding antibiotic resistance mechanisms is central to the development of anti-infective therapies and genomics-based drug discovery. Yet, many knowledge gaps remain regarding the resistance strategies employed against novel types of antibiotics from less-explored producers such as anaerobic bacteria, among them the Clostridia. Through the use of genome editing and functional assays, we found that CtaZ confers self-resistance against the copper chelator and gyrase inhibitor closthioamide (CTA) in Ruminiclostridium cellulolyticum. Bioinformatics, biochemical analyses, and X-ray crystallography revealed CtaZ as a founding member of a new group of GyrI-like proteins. CtaZ is unique in binding a polythioamide scaffold in a ligand-optimized hydrophobic pocket, thereby confining CTA. By genome mining using CtaZ as a handle, we discovered previously overlooked homologs encoded by diverse members of the phylum Firmicutes, including many pathogens. In addition to characterizing both a new role for a GyrI-like domain in self-resistance and unprecedented thioamide binding, this work aids in uncovering related drug-resistance mechanisms.
MeSH term(s)	Anti-Bacterial Agents/chemistry ; Bacteria, Anaerobic/genetics ; Carrier Proteins/genetics ; Drug Resistance, Microbial ; Gene Editing
Chemical Substances	Anti-Bacterial Agents ; Carrier Proteins
Language	English
Publishing date	2022-08-03
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202206168
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: An Unexpected Split-Merge Pathway in the Assembly of the Symmetric Nonribosomal Peptide Antibiotic Closthioamide.

Dunbar, Kyle L / Dell, Maria / Molloy, Evelyn M / Büttner, Hannah / Kumpfmüller, Jana / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2020 Volume 60, Issue 8, Page(s) 4104–4109

Abstract: Closthioamide (CTA) is a symmetric nonribosomal peptide (NRP) comprised of two diaminopropane-linked polythioamidated monomers. CTA is biosynthesized by Ruminiclostridium cellulolyticum via an atypical NRP synthetase (NRPS)-independent biosynthetic ... ...

Abstract	Closthioamide (CTA) is a symmetric nonribosomal peptide (NRP) comprised of two diaminopropane-linked polythioamidated monomers. CTA is biosynthesized by Ruminiclostridium cellulolyticum via an atypical NRP synthetase (NRPS)-independent biosynthetic pathway. Although the logic for monomer assembly was recently elucidated, the strategy for the biosynthesis and incorporation of the diamine linker remained a mystery. By means of genome editing, synthesis, and in vitro biochemical assays, we demonstrate that the final steps in CTA maturation proceed through a surprising split-merge pathway involving the dual use of a thiotemplated intermediate. This pathway includes the first examples of an aldo-keto reductase catalyzing the reductive release of a thiotemplated product, and of a transthioamidating transglutaminase. In addition to clarifying the remaining steps in CTA assembly, our data shed light on largely unexplored pathways for NRPS-independent peptide biosynthesis.
MeSH term(s)	Aldo-Keto Reductases/genetics ; Aldo-Keto Reductases/metabolism ; Anti-Bacterial Agents/analysis ; Anti-Bacterial Agents/biosynthesis ; Anti-Bacterial Agents/chemistry ; Biocatalysis ; Chromatography, High Pressure Liquid ; Clostridiales/genetics ; Clostridiales/metabolism ; Gene Editing ; Multigene Family ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Thioamides/analysis ; Thioamides/chemistry ; Thioamides/metabolism ; Transaminases/genetics ; Transaminases/metabolism ; Transglutaminases/genetics ; Transglutaminases/metabolism
Chemical Substances	Anti-Bacterial Agents ; Thioamides ; closthioamide ; Aldo-Keto Reductases (EC 1.1.1.-) ; Transglutaminases (EC 2.3.2.13) ; Transaminases (EC 2.6.1.-)
Language	English
Publishing date	2020-12-23
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202011741
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Analysis of Rhizonin Biosynthesis Reveals Origin of Pharmacophoric Furylalanine Moieties in Diverse Cyclopeptides.

Ehinger, Friedrich J / Niehs, Sarah P / Dose, Benjamin / Dell, Maria / Krabbe, Jana / Pidot, Sacha J / Stinear, Timothy P / Scherlach, Kirstin / Ross, Claudia / Lackner, Gerald / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2023 Volume 62, Issue 42, Page(s) e202308540

Abstract: Rhizonin A and B are hepatotoxic cyclopeptides produced by bacterial endosymbionts (Mycetohabitans endofungorum) of the fungus Rhizopus microsporus. Their toxicity critically depends on the presence of 3-furylalanine (Fua) residues, which also occur in ... ...

Abstract	Rhizonin A and B are hepatotoxic cyclopeptides produced by bacterial endosymbionts (Mycetohabitans endofungorum) of the fungus Rhizopus microsporus. Their toxicity critically depends on the presence of 3-furylalanine (Fua) residues, which also occur in pharmaceutically relevant cyclopeptides of the endolide and bingchamide families. The biosynthesis and incorporation of Fua by non-ribosomal peptide synthetases (NRPS), however, has remained elusive. By genome sequencing and gene inactivation we elucidated the gene cluster responsible for rhizonin biosynthesis. A suite of isotope labeling experiments identified tyrosine and l-DOPA as Fua precursors and provided the first mechanistic insight. Bioinformatics, mutational analysis and heterologous reconstitution identified dioxygenase RhzB as necessary and sufficient for Fua formation. RhzB is a novel type of heme-dependent aromatic oxygenases (HDAO) that enabled the discovery of the bingchamide biosynthesis gene cluster through genome mining.
MeSH term(s)	Humans ; Peptides, Cyclic/chemistry ; Computational Biology ; Multigene Family ; Fungi/metabolism ; Peptide Synthases/genetics ; Peptide Synthases/metabolism
Chemical Substances	Peptides, Cyclic ; Peptide Synthases (EC 6.3.2.-)
Language	English
Publishing date	2023-09-13
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202308540
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Reconstitution of Iterative Thioamidation in Closthioamide Biosynthesis Reveals Tailoring Strategy for Nonribosomal Peptide Backbones.

Dunbar, Kyle L / Dell, Maria / Molloy, Evelyn M / Kloss, Florian / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2019 Volume 58, Issue 37, Page(s) 13014–13018

Abstract: Thioamide-containing nonribosomal peptides (NRPs) are exceedingly rare. Recently the biosynthetic gene cluster for the thioamidated NRP antibiotic closthioamide (CTA) was reported, however, the enzyme responsible for and the timing of thioamide formation ...

Abstract	Thioamide-containing nonribosomal peptides (NRPs) are exceedingly rare. Recently the biosynthetic gene cluster for the thioamidated NRP antibiotic closthioamide (CTA) was reported, however, the enzyme responsible for and the timing of thioamide formation remained enigmatic. Here, genome editing, biochemical assays, and mutational studies are used to demonstrate that an Fe-S cluster containing member of the adenine nucleotide α-hydrolase protein superfamily (CtaC) is responsible for sulfur incorporation during CTA biosynthesis. However, unlike all previously characterized members, CtaC functions in a thiotemplated manner. In addition to prompting a revision of the CTA biosynthetic pathway, the reconstitution of CtaC provides the first example of a NRP thioamide synthetase. Finally, CtaC is used as a bioinformatic handle to demonstrate that thioamidated NRP biosynthetic gene clusters are more widespread than previously appreciated.
MeSH term(s)	Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biosynthetic Pathways ; Clostridiales/chemistry ; Clostridiales/genetics ; Clostridiales/metabolism ; Genes, Bacterial ; Multigene Family ; Peptide Synthases/genetics ; Peptide Synthases/metabolism ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Thioamides/chemistry ; Thioamides/metabolism
Chemical Substances	Anti-Bacterial Agents ; Bacterial Proteins ; Peptides ; Thioamides ; closthioamide ; Peptide Synthases (EC 6.3.2.-)
Language	English
Publishing date	2019-08-07
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.201905992
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Genome Editing Reveals Novel Thiotemplated Assembly of Polythioamide Antibiotics in Anaerobic Bacteria.

Dunbar, Kyle L / Büttner, Hannah / Molloy, Evelyn M / Dell, Maria / Kumpfmüller, Jana / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2018 Volume 57, Issue 43, Page(s) 14080–14084

Abstract: Closthioamide (CTA) is a unique symmetric nonribosomal peptide with six thioamide moieties that is produced by the Gram-positive obligate anaerobe Ruminiclostridium cellulolyticum. CTA displays potent inhibitory activity against important clinical ... ...

Abstract	Closthioamide (CTA) is a unique symmetric nonribosomal peptide with six thioamide moieties that is produced by the Gram-positive obligate anaerobe Ruminiclostridium cellulolyticum. CTA displays potent inhibitory activity against important clinical pathogens, making it a promising drug candidate. Yet, the biosynthesis of this DNA gyrase-targeting antibiotic has remained enigmatic. Using a combination of genome mining, genome editing (targeted group II intron, CRISPR/Cas9), and heterologous expression, we show that CTA biosynthesis involves specialized enzymes for starter unit biosynthesis, amide bond formation, thionation, and dimerization. Surprisingly, CTA biosynthesis involves a novel thiotemplated peptide assembly line that markedly differs from known nonribosomal peptide synthetases. These findings provide the first insights into the biosynthesis of thioamide-containing nonribosomal peptides and offer a starting point for the discovery of related natural products.
MeSH term(s)	Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Bacteria, Anaerobic/chemistry ; Bacteria, Anaerobic/genetics ; CRISPR-Cas Systems ; Carbon-13 Magnetic Resonance Spectroscopy ; Chromatography, High Pressure Liquid ; Clostridiales/chemistry ; Clostridiales/genetics ; DNA Gyrase/drug effects ; Gene Editing ; Genes, Bacterial ; Introns ; Mass Spectrometry ; Multigene Family ; Peptide Synthases/chemistry ; Proton Magnetic Resonance Spectroscopy ; Thioamides/chemistry ; Thioamides/pharmacology
Chemical Substances	Anti-Bacterial Agents ; Thioamides ; DNA Gyrase (EC 5.99.1.3) ; Peptide Synthases (EC 6.3.2.-) ; non-ribosomal peptide synthase (EC 6.3.2.-)
Language	English
Publishing date	2018-10-03
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.201807970
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

To top

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito