Evidence map›Paper›PMID 22332716›Full record

ReviewCritical reviews in biochemistry and molecular biology

The dynamic determinants of reaction specificity in the IMPDH/GMPR family of (β/α)(8) barrel enzymes.

Lizbeth Hedstrom

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  11. Molecular Mechanisms of Enzyme Activation by Monovalent Cations.The Journal of biological chemistry · 2016
    Review
  12. Article
  13. 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

1 author at 1 institution in 1 country.

Lizbeth HedstromDepartments of Biology and Chemistry, Brandeis University, Waltham, MA 02454, USA. hedstrom@brandeis.edu
Brandeis University · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
INOSINE MONOPHOSPHATE DEHYDROGENASER01GM054403 · NIGMS · BRANDEIS UNIVERSITY · PI HEDSTROM, LIZBETH K. · 1998 to 2016
$4.2M
NCRR NIH HHS P41 RR001081NIGMS NIH HHS GM054403NIGMS NIH HHS R01 GM054403
6 · The paper itself

Abstract

The inosine monophosphate dehydrogenase (IMPDH)/guanosine monophosphate reductase (GMPR) family of (β/α)(8) enzymes presents an excellent opportunity to investigate how subtle changes in enzyme structure change reaction specificity. IMPDH and GMPR bind the same ligands with similar affinities and share a common set of catalytic residues. Both enzymes catalyze a hydride transfer reaction involving a nicotinamide cofactor hydride, and both reactions proceed via the same covalent intermediate. In the case of IMPDH, this intermediate reacts with water, while in GMPR it reacts with ammonia. In both cases, the two chemical transformations are separated by a conformational change. In IMPDH, the conformational change involves a mobile protein flap while in GMPR, the cofactor moves. Thus reaction specificity is controlled by differences in dynamics, which in turn are controlled by residues outside the active site. These findings have some intriguing implications for the evolution of the IMPDH/GMPR family.

Indexed as

AmmoniaCatalytic DomainCations, MonovalentGMP ReductaseGuanosine MonophosphateHumansIMP DehydrogenaseKineticsLigandsProtein BindingProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySubstrate SpecificityWaterAmmoniaCations, MonovalentGMPR2 protein, humanGMP ReductaseGuanosine MonophosphateIMP DehydrogenaseIMPDH2 protein, humanLigandsWater

Identifiers

PMID22332716
PMCPMC3337344
OpenAlexW2030153345

What OpenQuestion holds

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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.