Evidence map›Paper›PMID 31593192›Full record

ReviewNatural product reports2020

Type II non-ribosomal peptide synthetase proteins: structure, mechanism, and protein-protein interactions.

Matt J Jaremko, Tony D Davis, Joshua C Corpuz, Michael D Burkart

Open access · greenAbstract readReview
In one paragraph

Review in Natural product reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Article
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Compilation of the Antimicrobial Compounds Produced byMolecules (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Matt J JaremkoDepartment of Chemistry and Biochemistry, University of California, 9500 Gilman Drive, La Jolla, San Diego, California 92093-0358, USA. mburkart@ucsd.edu.
Tony D DavisDepartment of Chemistry and Biochemistry, University of California, 9500 Gilman Drive, La Jolla, San Diego, California 92093-0358, USA. mburkart@ucsd.edu.ORCID 0000-0001-5629-7075
Joshua C CorpuzDepartment of Chemistry and Biochemistry, University of California, 9500 Gilman Drive, La Jolla, San Diego, California 92093-0358, USA. mburkart@ucsd.edu.ORCID 0000-0002-0106-3500
Michael D BurkartDepartment of Chemistry and Biochemistry, University of California, 9500 Gilman Drive, La Jolla, San Diego, California 92093-0358, USA. mburkart@ucsd.edu.ORCID 0000-0002-4472-2254
University of California System · US

Funding

UCSD/SDSU IRACDAK12GM068524 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TREJO, JOANN · 2003 to 2025
$24.4M
Contemporary Approaches to Cancer Cell Signaling and CommunicationT32CA009523 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DONOGHUE, DANIEL J, YANG, JING · 1985 to 2025
$12.1M
MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Protein-Protein Interactions in Natural Product BiosynthesisR01GM095970 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2012 to 2025
$5.9M
Regulation of Receptor Tyrosine KinasesR01GM065490 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI DONOGHUE, DANIEL J · 2002 to 2005
$1.0M
Interrogation of Microbial Natural Product MethyltransferasesK99GM129454 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DAVIS, TONY D. · 2019 to 2019
$93k
NCI NIH HHS T32 CA009523NIGMS NIH HHS K12 GM068524NIGMS NIH HHS K99 GM129454NIGMS NIH HHS R01 GM065490NIGMS NIH HHS R01 GM095970NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

Covering: 1990 to 2019 Many medicinally-relevant compounds are derived from non-ribosomal peptide synthetase (NRPS) products. Type I NRPSs are organized into large modular complexes, while type II NRPS systems contain standalone or minimal domains that often encompass specialized tailoring enzymes that produce bioactive metabolites. Protein-protein interactions and communication between the type II biosynthetic machinery and various downstream pathways are critical for efficient metabolite production. Importantly, the architecture of type II NRPS proteins makes them ideal targets for combinatorial biosynthesis and metabolic engineering. Future investigations exploring the molecular basis or protein-protein recognition in type II NRPS pathways will guide these engineering efforts. In this review, we consolidate the broad range of NRPS systems containing type II proteins and focus on structural investigations, enzymatic mechanisms, and protein-protein interactions important to unraveling pathways that produce unique metabolites, including dehydrogenated prolines, substituted benzoic acids, substituted amino acids, and cyclopropanes.

Indexed as

Amino AcidsBenzoic AcidCyclopropanesHydroxylationLactamsMacrolidesNetropsinPeptide SynthasesProlineProtein Interaction MapsPyrrolesThiazolesThionesAmino AcidsBenzoic AcidCyclopropanesLactamsleinamycinMacrolidesNetropsinnon-ribosomal peptide synthasePeptide SynthasesProlinePyrrolesThiazolesThiones

Identifiers

PMID31593192
PMCPMC7101270
OpenAlexW2980170245

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.