Evidence map›Paper›PMID 25210039›Full record

ReviewThe Journal of biological chemistry2014

Enzyme promiscuity: engine of evolutionary innovation.

Chetanya Pandya, Jeremiah D Farelli, Debra Dunaway-Mariano, Karen N Allen

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed.

  1. Review
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8 more citing papers are in PubMed but not listed here.

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

4 authors.

Chetanya PandyaBioinformatics Graduate Program and Boston University, Boston, Massachusetts 02215.
Jeremiah D FarelliDepartment of Chemistry, Boston University, Boston, Massachusetts 02215 and.
Debra Dunaway-MarianoDepartment of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131. Electronic address: dd39@unm.edu.
Karen N AllenBioinformatics Graduate Program and Boston University, Boston, Massachusetts 02215; Department of Chemistry, Boston University, Boston, Massachusetts 02215 and. Electronic address: drkallen@bu.edu.

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 2010 to 2015
$34.6M
Structure and Function of HAD Phosphatase Partners Dullard and LipinR01GM098760 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI ALLEN, KAREN N., DUNAWAY-MARIANO, DEBRA · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM098760NIGMS NIH HHS U54 GM093342
6 · The paper itself

Abstract

Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal to the successful acquisition of novel biological functions. Action on multiple substrates (substrate ambiguity) can be harnessed for performance of functions in the cell that supersede catalysis of a single metabolite. These functions include proofreading, scavenging of nutrients, removal of antimetabolites, balancing of metabolite pools, and establishing system redundancy. In this review, we present examples of enzymes that perform these cellular roles by leveraging substrate ambiguity and then present the structural features that support both specificity and ambiguity. We focus on the phosphatases of the haloalkanoate dehalogenase superfamily and the thioesterases of the hotdog fold superfamily.

Indexed as

Evolution, MolecularAnimalsBiocatalysisCatalytic DomainEnzymesHumansModels, MolecularSubstrate SpecificityEnzymesEnzyme CatalysisHydrolasePhosphataseProtein EvolutionStructural Biology

Identifiers

PMID25210039
PMCPMC4215207

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.