Evidence map›Paper›PMID 35644170›Full record

ArticleMethods in enzymology2022

Using kinetic isotope effects to probe the mechanism of adenosylcobalamin-dependent enzymes.

E Neil G Marsh

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2022. 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
1.0field-weighted citation impact, top 30% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

1 author at 1 institution in 1 country.

E Neil G MarshDepartment of Chemistry, University of Michigan, Ann Arbor, MI, United States; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, United States. Electronic address: nmarsh@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Understanding hydrogen atom transfer reactions in enzymesR01GM093088 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARSH, E NEIL · 2010 to 2023
$3.5M
NIGMS NIH HHS R01 GM093088
6 · The paper itself

Abstract

Adenosylcobalamin- (AdoCbl) dependent enzyme reactions involved the transfer of hydrogen atoms between the 5'-carbon of the coenzyme and the substrates and products of the reaction. Tritium and deuterium kinetic isotope effect measurements are, therefore, a valuable tool to probe the mechanisms of AdoCbl-dependent enzymes, as they can provide information about the reaction pathway and the rate-determining step. Furthermore, if the intrinsic kinetic isotope effect can be isolated, information on the nature of the transition state associated with hydrogen transfer can be obtained. In this chapter I present methods for the preparation of isotopically-labeled AdoCbl and their use in rapid chemical quench experiments that allow isotope effects on specific steps in the reaction to be isolated. These techniques are illustrated with examples from my laboratory's studies on the AdoCbl dependent enzyme, glutamate mutase.

Indexed as

CobamidesIsotopesHydrogenKineticscobamamideCobamidesHydrogenIsotopes(14)C-labeled AdoCblGlutamate mutaseRapid chemical quenchSecondary isotope effectsTritium-labeled AdoCblTritium partitioning

Identifiers

PMID35644170
PMCPMC11141886
OpenAlexW4210484728

What OpenQuestion holds

Textmetadata
LicenceTDM
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.