Evidence map›Paper›PMID 28696108›Full record

ArticleThe journal of physical chemistry. B2017

Incorporating Fast Protein Dynamics into Enzyme Design: A Proposed Mutant Aromatic Amine Dehydrogenase.

Ioanna Zoi, Dimitri Antoniou, Steven D Schwartz

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023
    Review
  2. Article
  3. Review
  4. Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022
    Review
  5. Article
  6. Article
  7. Heavy Enzymes and the Rational Redesign of Protein Catalysts.Chembiochem : a European journal of chemical biology · 2019
    Article
  8. 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.

Ioanna ZoiDepartment of Chemistry and Biochemistry, University of Arizona , 1306 East University Boulevard, Tucson, Arizona 85721, United States.
Dimitri AntoniouDepartment of Chemistry and Biochemistry, University of Arizona , 1306 East University Boulevard, Tucson, Arizona 85721, United States.
Steven D SchwartzDepartment of Chemistry and Biochemistry, University of Arizona , 1306 East University Boulevard, Tucson, Arizona 85721, United States.ORCID 0000-0002-0308-1059

Funding

Proton Transfer Dynamics in Heme-Copper OxidasesP01GM068036 · NIGMS · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI CALLENDER, ROBERT · 2004 to 2018
$26.4M
NIGMS NIH HHS P01 GM068036
6 · The paper itself

Abstract

In recent years, there has been encouraging progress in the engineering of enzymes that are designed to catalyze reactions not accelerated by natural enzymes. We tested the possibility of reengineering an existing enzyme by introducing a fast protein motion that couples to the reaction. Aromatic amine dehydrogenase is a system that has been shown to use a fast substrate motion as part of the reaction mechanism. We identified a mutation that preserves this fast motion but also introduces a favorable fast motion near the active site that did not exist in the native enzyme. Transition path sampling was used for the analysis of the atomic details of the mechanism.

Indexed as

BiocatalysisCatalytic DomainModels, MolecularOxidoreductases Acting on CH-NH Group DonorsProtein EngineeringQuantum TheorySubstrate SpecificityTryptaminesaromatic amine dehydrogenaseOxidoreductases Acting on CH-NH Group DonorstryptamineTryptamines

Identifiers

PMID28696108
PMCPMC5763476

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.