Evidence map›Paper›PMID 25771539›Full record

ArticleThe Journal of biological chemistry2015

Kinetic mechanism of protein N-terminal methyltransferase 1.

Stacie L Richardson, Yunfei Mao, Gang Zhang, Pahul Hanjra, Darrell L Peterson, Rong Huang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

38 citing papers in PubMed, 49 citations in OpenAlex.

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  18. Mechanisms and inhibitors of nicotinamideRSC medicinal chemistry · 2021
    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

6 authors at 1 institution in 1 country.

Stacie L RichardsonFrom the Department of Medicinal Chemistry, the Institute for Structural Biology and Drug Discovery, and.
Yunfei MaoFrom the Department of Medicinal Chemistry, the Institute for Structural Biology and Drug Discovery, and.
Gang ZhangFrom the Department of Medicinal Chemistry, the Institute for Structural Biology and Drug Discovery, and.
Pahul HanjraFrom the Department of Medicinal Chemistry, the Institute for Structural Biology and Drug Discovery, and.
Darrell L Petersonthe Institute for Structural Biology and Drug Discovery, and the Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, Virginia 23219.
Rong HuangFrom the Department of Medicinal Chemistry, the Institute for Structural Biology and Drug Discovery, and rhuang@vcu.edu.
Virginia Commonwealth University · US

Funding

Center for Clinical and Translational ResearchUL1TR000058 · NCATS · VIRGINIA COMMONWEALTH UNIVERSITY · PI MOELLER, FREDERICK GERARD · 2012 to 2015
$12.5M
NCATS NIH HHS UL1 TR000058NCATS NIH HHS UL1TR000058
6 · The paper itself

Abstract

The protein N-terminal methyltransferase 1 (NTMT1) catalyzes the transfer of the methyl group from the S-adenosyl-l-methionine to the protein α-amine, resulting in formation of S-adenosyl-l-homocysteine and α-N-methylated proteins. NTMT1 is an interesting potential anticancer target because it is overexpressed in gastrointestinal cancers and plays an important role in cell mitosis. To gain insight into the biochemical mechanism of NTMT1, we have characterized the kinetic mechanism of recombinant NTMT1 using a fluorescence assay and mass spectrometry. The results of initial velocity, product, and dead-end inhibition studies indicate that methylation by NTMT1 proceeds via a random sequential Bi Bi mechanism. In addition, our processivity studies demonstrate that NTMT1 proceeds via a distributive mechanism for multiple methylations. Together, our studies provide new knowledge about the kinetic mechanism of NTMT1 and lay the foundation for the development of mechanism-based inhibitors.

Indexed as

Amino Acid SequenceBiocatalysisEnzyme InhibitorsHumansKineticsMethylationProtein MethyltransferasesEnzyme InhibitorsProtein MethyltransferasesDistributive MechanismEnzyme KineticsEnzyme MechanismEnzyme ProcessingEpigeneticsPost-translational Modification (PTM)Protein MethylationProtein N-terminal Methyltransferase

Identifiers

PMID25771539
PMCPMC4416863
OpenAlexW2051515034

What OpenQuestion holds

Textmetadata
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.