Evidence map›Paper›PMID 21401078›Full record

ArticleBiochemistry2011

Substrate binding and reactivity are not linked: grafting a proton-transfer network into a Class 1A dihydroorotate dehydrogenase.

Claudia A McDonald, Bruce A Palfey

Abstract 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. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Claudia A McDonaldDepartment of Biological Chemistry, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0606, United States.
Bruce A Palfey

Funding

Mechanisms of Dihydroorotate DehydrogenasesR01GM061087 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PALFEY, BRUCE A · 2002 to 2011
$2.1M
NIGMS NIH HHS GM61087NIGMS NIH HHS GM61087-08-S1NIGMS NIH HHS R01 GM061087
6 · The paper itself

Abstract

Adding the two residues comprising the conserved proton-transfer network of Class 2 dihydroorotate dehydrogenase (DHOD) to the Cys130Ser Class 1A DHOD did not restore the function of the active site base or rapid flavin reduction. Studies of triple, double, and single mutant Class 1A enzymes showed that the network actually prevents cysteine from acting as a base and that the network residues act independently. Our data show that residue 71 is an important determinant of ligand binding specificity. The Leu71Phe mutation tightens dihydrooroate binding but weakens the binding of benzoate inhibitors of Class 1A enzymes.

Indexed as

Bacterial ProteinsBinding SitesBiocatalysisDihydroorotate DehydrogenaseKineticsLactococcus lactisModels, ChemicalModels, MolecularMolecular StructureMutationOrotic AcidOxidation-ReductionOxidoreductases Acting on CH-CH Group DonorsProtein BindingProtein Structure, TertiaryProtons4,5-dihydroorotic acidBacterial ProteinsDihydroorotate DehydrogenaseOrotic AcidOxidoreductases Acting on CH-CH Group DonorsProtons

Identifiers

PMID21401078
PMCPMC3077728

What OpenQuestion holds

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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.