Evidence map›Paper›PMID 35224236›Full record

ReviewSynthetic and systems biotechnology2022

Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains.

Joshua C Corpuz, Javier O Sanlley, Michael D Burkart

Abstract readReview
In one paragraph

Review in Synthetic and systems biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. Pathway and protein engineering for biosynthesis.Synthetic and systems biotechnology · 2022
    Article
  15. Article
  16. 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

3 authors.

Joshua C CorpuzDepartment of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA.
Javier O SanlleyDepartment of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA.
Michael D BurkartDepartment of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA.

Funding

Protein-Protein Interactions in Natural Product BiosynthesisR01GM095970 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2012 to 2025
$5.9M
Creating natural product diversity via the fabrication of a hybrid fatty acid-nonribosomal peptide synthetaseF31GM137616 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CORPUZ, JOSHUA CATUNGAL · 2021 to 2022
$59k
NIGMS NIH HHS F31 GM137616NIGMS NIH HHS R01 GM095970
6 · The paper itself

Abstract

Non-ribosomal peptide synthetases (NRPSs) are attractive targets for biosynthetic pathway engineering due to their modular architecture and the therapeutic relevance of their products. With catalysis mediated by specific protein-protein interactions formed between the peptidyl carrier protein (PCP) and its partner enzymes, NRPS enzymology and control remains fertile ground for discovery. This review focuses on the recent efforts within structural biology by compiling high-resolution structural data that shed light into the various protein-protein interfaces formed between the PCP and its partner enzymes, including the phosphopantetheinyl transferase (PPTase), adenylation (A) domain, condensation (C) domain, thioesterase (TE) domain and other tailoring enzymes within the synthetase. Integrating our understanding of how the PCP recognizes partner proteins with the potential to use directed evolution and combinatorial biosynthetic methods will enhance future efforts in discovery and production of new bioactive compounds.

Indexed as

Combinatorial biosynthesisNatural productsNon-ribosomal peptide synthetasePeptidyl carrier proteinProtein-protein interactionsSynthetic biology

Identifiers

PMID35224236
PMCPMC8857579

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.