Evidence map›Paper›PMID 27635101›Full record

ArticleIsrael journal of chemistry2015

Mechanistic Enzymology of the Radical SAM Enzyme DesII.

Mark W Ruszczycky, Hung-Wen Liu

Abstract read
In one paragraph

Article in Israel journal of chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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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

2 authors.

Mark W RuszczyckyDivision of Medicinal Chemistry, College of Pharmacy, University of Texas at Austin, Austin, Texas 78712, United States.
Hung-Wen LiuDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.

Funding

Mechanistic Studies of Deoxy Sugar BiosynthesisR01GM035906 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI LIU, HUNG-WEN · 1986 to 2023
$6.1M
MECHANISMS OF BIOSYNTHETIC FORMATION OF DEOXY SUGARSR37GM035906 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIU, HUNG-WEN · 1999 to 2008
$3.4M
NIGMS NIH HHS R01 GM035906NIGMS NIH HHS R37 GM035906
6 · The paper itself

Abstract

DesII is a member of the radical SAM family of enzymes that catalyzes radical-mediated transformations of TDP-4-amino-4,6-didexoy-D-glucose as well as other sugar nucleotide diphosphates. Like nearly all radical SAM enzymes, the reactions begin with the reductive homolysis of SAM to produce a 5'-deoxyadenosyl radical which is followed by regiospecific hydrogen atom abstraction from the substrate. What happens next, however, depends on the nature of the substrate radical so produced. In the case of the biosynthetically relevant substrate, a radical-mediated deamination ensues; however, when this amino group is replaced with a hydroxyl, one instead observes dehydrogenation. The factors that govern the fate of the initially generated substrate radical as well as the mechanistic details underlying these transformations have been a key focus of research into the chemistry of DesII. This review will discuss recent discoveries pertaining to the enzymology of DesII, how it may relate to understanding other radical-mediated lyases and dehydrogenases and the working hypotheses currently being investigated regarding the mechanism of DesII catalysis.

Indexed as

CarbohydratesDeaminationDehydrogenationEnzyme CatalysisRadical Reactions

Identifiers

PMID27635101
PMCPMC5021314

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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.