Evidence map›Paper›PMID 25219626›Full record

ReviewArchives of biochemistry and biophysics2014

Identification and characterization of new family members in the tautomerase superfamily: analysis and implications.

Jamison P Huddleston, Elizabeth A Burks, Christian P Whitman

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  7. Environmental adaptation ofInternational journal of biological sciences · 2018
    Article
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  9. Review
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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 at 1 institution in 1 country.

Jamison P HuddlestonDivision of Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX 78712, United States.
Elizabeth A BurksDivision of Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX 78712, United States.
Christian P WhitmanDivision of Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX 78712, United States. Electronic address: whitman@austin.utexas.edu.
The University of Texas at Austin · US

Funding

ENZYMES OF THE META-FISSION PATHWAYR01GM041239 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI WHITMAN, CHRISTIAN P. · 1995 to 2017
$3.0M
Structure and Mechanism in the Tautomerase SuperfamilyR01GM065324 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI WHITMAN, CHRISTIAN P. · 2002 to 2011
$2.3M
NIGMS NIH HHS R01 GM041239NIGMS NIH HHS R01 GM065324NIGMS NIH HHS R01 GM41239NIGMS NIH HHS R01 GM65324
6 · The paper itself

Abstract

Tautomerase superfamily members are characterized by a β-α-β building block and a catalytic amino terminal proline. 4-Oxalocrotonate tautomerase (4-OT) and malonate semialdehyde decarboxylase (MSAD) are the title enzymes of two of the five known families in the superfamily. Two recent developments in these families indicate that there might be more metabolic diversity in the tautomerase superfamily than previously thought. 4-OT homologues have been identified in three biosynthetic pathways, whereas all previously characterized 4-OTs are found in catabolic pathways. In the MSAD family, homologues have been characterized that lack decarboxylase activity, but have a modest hydratase activity using 2-oxo-3-pentynoate. This observation stands in contrast to the first characterized MSAD, which is a proficient decarboxylase and a less efficient hydratase. The hydratase activity was thought to be a vestigial and promiscuous activity. However, this recent discovery suggests that the hydratase activity might reflect a new activity in the MSAD family for an unknown substrate. These discoveries open up new avenues of research in the tautomerase superfamily.

Indexed as

Structural Homology, ProteinBacteriaBacterial ProteinsCarboxy-LyasesIsomerases4-oxalocrotonate tautomeraseBacterial ProteinsCarboxy-LyasesIsomerasesmalonate semialdehyde decarboxylase4-Oxalocrotonate tautomeraseCatalytic amino terminal prolineCatalytic promiscuityHydratase activityMalonate semialdehyde decarboxylaseTautomerase superfamilyβ–α–β fold

Identifiers

PMID25219626
PMCPMC4258425
OpenAlexW2073672841

What OpenQuestion holds

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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.