Evidence map›Paper›PMID 27791059›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Scaffoldless engineered enzyme assembly for enhanced methanol utilization.

J Vincent Price, Long Chen, W Brian Whitaker, Eleftherios Papoutsakis, Wilfred Chen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
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  8. Perspectives for Using COBioengineering (Basel, Switzerland) · 2023
    Review
  9. Review
  10. Article
  11. Application of artificial scaffold systems in microbial metabolic engineering.Frontiers in bioengineering and biotechnology · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Bioconversion of Methanol by Synthetic Methylotrophy.Advances in biochemical engineering/biotechnology · 2022
    Article
  17. Strategies for Multienzyme Assemblies.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  18. Review
  19. Article
  20. Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy.Frontiers in bioengineering and biotechnology · 2021
    Review
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

5 authors at 2 institutions in 1 country.

J Vincent PriceDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716.
Long ChenDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716.
W Brian WhitakerDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716.
Eleftherios PapoutsakisDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716.
Wilfred ChenDepartment of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716; wilfred@udel.edu.
University of Delaware · USBiotechnology Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methanol is an important feedstock derived from natural gas and can be chemically converted into commodity and specialty chemicals at high pressure and temperature. Although biological conversion of methanol can proceed at ambient conditions, there is a dearth of engineered microorganisms that use methanol to produce metabolites. In nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction. Thus, efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism. An emerging strategy to promote efficient substrate channeling is to spatially organize pathway enzymes in an engineered assembly to provide kinetic driving forces that promote carbon flux in a desirable direction. Here, we report a scaffoldless, self-assembly strategy to organize Mdh, Hps, and Phi into an engineered supramolecular enzyme complex using an SH3-ligand interaction pair, which enhances methanol conversion to fructose-6-phosphate (F6P). To increase methanol consumption, an "NADH Sink" was created using

Indexed as

methanemethylotophsscaffoldsubstrate channelingsupramolcular

Identifiers

PMID27791059
PMCPMC5111641
OpenAlexW2536714764

What OpenQuestion holds

Textmetadata
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.