Evidence map›Paper›PMID 22480290›Full record

ArticleJournal of the American Chemical Society2012

Biochemical and structural characterization of germicidin synthase: analysis of a type III polyketide synthase that employs acyl-ACP as a starter unit donor.

Joseph A Chemler, Tonia J Buchholz, Todd W Geders, David L Akey, Christopher M Rath, George E Chlipala, Janet L Smith, David H Sherman

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The virulome ofMicrobial genomics · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Biosynthesis of Polyketides inMicroorganisms · 2019
    Review
  9. Genome mining reveals uncommon alkylpyrones as type III PKS products from myxobacteria.Journal of industrial microbiology & biotechnology · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Germicidins H-J from Streptomyces sp. CB00361.The Journal of antibiotics · 2017
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

8 authors at 3 institutions in 2 countries.

Joseph A ChemlerLife Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA.
Tonia J Buchholz
Todd W Geders
David L Akey
Christopher M Rath
George E Chlipala
Janet L Smith
David H Sherman
University of Michigan–Ann Arbor · USBipar · FRPurdue University West Lafayette · US

Funding

STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
Molecular Analysis of Modular Polyketide SynthasesR01GM076477 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHERMAN, DAVID H, SMITH, JANET L. · 2006 to 2018
$5.2M
GLUTAMINE AMIDOTRANSFERASES AND PARTNER ENZYMESR37DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1998 to 2007
$2.4M
Engineering hybrid polyketide synthase systems using high affinity DNA binding doF32GM095065 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEMLER, JOSEPH ANTHONY · 2011 to 2012
$101k
NIDDK NIH HHS DK42303NIDDK NIH HHS R01 DK042303NIDDK NIH HHS R37 DK042303NIGMS NIH HHS GM076477NIGMS NIH HHS GM095065NIGMS NIH HHS R01 GM076477
6 · The paper itself

Abstract

Germicidin synthase (Gcs) from Streptomyces coelicolor is a type III polyketide synthase (PKS) with broad substrate flexibility for acyl groups linked through a thioester bond to either coenzyme A (CoA) or acyl carrier protein (ACP). Germicidin synthesis was reconstituted in vitro by coupling Gcs with fatty acid biosynthesis. Since Gcs has broad substrate flexibility, we directly compared the kinetic properties of Gcs with both acyl-ACP and acyl-CoA. The catalytic efficiency of Gcs for acyl-ACP was 10-fold higher than for acyl-CoA, suggesting a strong preference toward carrier protein starter unit transfer. The 2.9 Å germicidin synthase crystal structure revealed canonical type III PKS architecture along with an unusual helical bundle of unknown function that appears to extend the dimerization interface. A pair of arginine residues adjacent to the active site affect catalytic activity but not ACP binding. This investigation provides new and surprising information about the interactions between type III PKSs and ACPs that will facilitate the construction of engineered systems for production of novel polyketides.

Indexed as

Acyl Carrier ProteinAcyl Coenzyme ABacterial ProteinsCrystallography, X-RayModels, MolecularMutationPolyketide SynthasesProtein BindingPyronesSignal TransductionStreptomyces coelicolorSubstrate SpecificityAcyl Carrier ProteinAcyl Coenzyme ABacterial ProteinsgermicidinPolyketide SynthasesPyrones

Identifiers

PMID22480290
PMCPMC3342439
OpenAlexW1975825697

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.