Evidence map›Paper›PMID 23341455›Full record

ArticleThe Journal of biological chemistry2013

Catalysis by N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase (PIG-L) from Entamoeba histolytica: new roles for conserved residues.

Mohammad Ashraf, Perinthottathil Sreejith, Usha Yadav, Sneha Sudha Komath

Abstract read
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Article in The Journal of biological chemistry, 2013. 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

4 authors.

Mohammad AshrafSchool of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Perinthottathil SreejithSchool of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Usha YadavSchool of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Sneha Sudha KomathSchool of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. Electronic address: sskomath@mail.jnu.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We showed previously that Entamoeba histolytica PIG-L exhibits a novel metal-independent albeit metal-stimulated activity. Using mutational and biochemical analysis, here we identify Asp-46 and His-140 of the enzyme as being important for catalysis. We show that these mutations neither affect the global conformational of the enzyme nor alter its metal binding affinity. The defect in catalysis, due to the mutations, is specifically due to an effect on V(max) and not due to altered substrate affinity (or K(m)). We propose a general acid-base pair mechanism to explain our results.

Indexed as

Gene Expression Regulation, EnzymologicAmidohydrolasesCatalysisCircular DichroismEntamoeba histolyticaEscherichia coliGlycomicsHydrogen-Ion ConcentrationKineticsMetalsModels, BiologicalModels, ChemicalMutagenesis, Site-DirectedMutationProtein ConformationProtein Structure, TertiaryAmidohydrolasesMetalsN-acetylglucosaminyl-phosphatidylinositol de-N-acetylase

Identifiers

PMID23341455
PMCPMC3597800

What OpenQuestion holds

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Registered trials

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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.