Evidence map›Paper›PMID 21473615›Full record

ArticleBiochemistry2011

Stochastic ensembles, conformationally adaptive teamwork, and enzymatic detoxification.

William M Atkins, Hong Qian

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
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  5. 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

2 authors at 1 institution in 1 country.

William M AtkinsDepartment of Medicinal Chemistry and Department of Applied Mathematics, University of Washington, Seattle, Washington 98190, United States. winky@uw.edu
Hong Qian
University of Washington · US

Funding

TOXIC DRUG INTERACTIONS WITH VALPROIC ACIDP01GM032165 · NIGMS · UNIVERSITY OF WASHINGTON · PI RETTIE, ALLAN EDWARD · 1985 to 2012
$18.3M
Glutathione S-Transferases and Oxidative StressR01GM062284 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 2002 to 2011
$2.0M
NIGMS NIH HHS GM32165NIGMS NIH HHS GM62284NIGMS NIH HHS P01 GM032165NIGMS NIH HHS R01 GM062284
6 · The paper itself

Abstract

It has been appreciated for a long time that enzymes exist as conformational ensembles throughout multiple stages of the reactions they catalyze, but there is renewed interest in the functional implications. The energy landscape that results from conformationlly diverse poteins is a complex surface with an energetic topography in multiple dimensions, even at the transition state(s) leading to product formation, and this represents a new paradigm. At the same time there has been renewed interest in conformational ensembles, a new paradigm concerning enzyme function has emerged, wherein catalytic promiscuity has clear biological advantages in some cases. "Useful", or biologically functional, promiscuity or the related behavior of "multifunctionality" can be found in the immune system, enzymatic detoxification, signal transduction, and the evolution of new function from an existing pool of folded protein scaffolds. Experimental evidence supports the widely held assumption that conformational heterogeneity promotes functional promiscuity. The common link between these coevolving paradigms is the inherent structural plasticity and conformational dynamics of proteins that, on one hand, lead to complex but evolutionarily selected energy landscapes and, on the other hand, promote functional promiscuity. Here we consider a logical extension of the overlap between these two nascent paradigms: functionally promiscuous and multifunctional enzymes such as detoxification enzymes are expected to have an ensemble landscape with more states accessible on multiple time scales than substrate specific enzymes. Two attributes of detoxification enzymes become important in the context of conformational ensembles: these enzymes metabolize multiple substrates, often in substrate mixtures, and they can form multiple products from a single substrate. These properties, combined with complex conformational landscapes, lead to the possibility of interesting time-dependent, or emergent, properties. Here we demonstrate these properties with kinetic simulations of nonequilibrium steady state (NESS) behavior resulting from energy landscapes expected for detoxification enzymes. Analogous scenarios with other promiscuous enzymes may be worthy of consideration.

Indexed as

Models, ChemicalATP Binding Cassette Transporter, Subfamily B, Member 1Biological Transport, ActiveCatalysisCytochrome P-450 Enzyme SystemGlucuronosyltransferaseInactivation, MetabolicLigandsProtein ConformationStochastic ProcessesSubstrate SpecificityATP Binding Cassette Transporter, Subfamily B, Member 1Cytochrome P-450 Enzyme SystemGlucuronosyltransferaseLigands

Identifiers

PMID21473615
PMCPMC3092024
OpenAlexW2084488431

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.