A continuous assay of acetate kinase activity: measurement of inorganic phosphate release generated by hydroxylaminolysis of acetyl phosphate.

Soma Mukhopadhyay, Miriam S Hasson, David A Sanders

Open access · greenAbstract readEvaluation Study

In one paragraph

Article in Bioorganic chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed, 5 citations in OpenAlex.

Direct detection of the acetate-forming activity of the enzyme acetate kinase.Journal of visualized experiments : JoVE · 2011
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

3 authors at 1 institution in 1 country.

Soma MukhopadhyayDepartment of Biological Sciences, Purdue University, 915 W. State Street, Room B-122, Lilly Hall, West Lafayette, IN 47907, USA.

Miriam S Hasson

David A Sanders

State Street (United States) · US

Funding

STRUCTURAL STUDY OF ENZYMIC PO3 TRANSFER--ACETATE KINASER01GM057056 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI HASSON, MIRIAM S · 1999 to 2002

$616k

NIGMS NIH HHS R01 GM057056NIGMS NIH HHS R01-GM57056

6 · The paper itself

Abstract

Acetate kinase, a member of the ASKHA (Acetate and Sugar Kinases, Hsp70, Actin) phosphotransferase superfamily is a central enzyme in prokaryotic carbon and energy metabolism. Recently extensive structural and biochemical studies of acetate kinase and related carboxylate kinases have been conducted. Analysis of the kinetic properties of wild-type and mutant enzymes has been impeded by the nature of the current assays for acetate kinase activity. These assays have the disadvantages of being either discontinuous or insensitive or of utilizing compounds that interfere with activity measurements. We have developed a novel continuous assay that depends on the purine nucleoside phosphorylase-based spectroscopic measurement of the inorganic phosphate generated by hydroxylaminolysis of one of the products of the acetate kinase reaction, acetyl phosphate. This assay has enabled a determination of the kinetic parameters of the Thermotoga maritima acetate kinase that indicates a lower K(m) for acetate than previously published.

Indexed as

Molecular Probe TechniquesAcetate KinaseHydroxylaminesKineticsOrganophosphatesPhosphatesSpectrum AnalysisThermotoga maritimaAcetate Kinaseacetyl phosphateHydroxylaminesOrganophosphatesPhosphates

Identifiers

PMID18294673

DOI10.1016/j.bioorg.2007.12.002

PMCPMC2376208

OpenAlexW1971800126

What OpenQuestion holds

Textmetadata

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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.