Evidence map›Paper›PMID 17165757›Full record

ArticleJournal of the American Chemical Society2006

Mechanism of benzylsuccinate synthase probed by substrate and isotope exchange.

Lei Li, E Neil G Marsh

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 35 citations in OpenAlex.

  1. The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Development of aniScience · 2023
    Article
  6. Article
  7. New tricks for the glycyl radical enzyme family.Critical reviews in biochemistry and molecular biology · 2017
    Review
  8. Article
  9. Article
  10. Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Review
  12. Adenosyl radical: reagent and catalyst in enzyme reactions.Chembiochem : a European journal of chemical biology · 2010
    Review
  13. 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

2 authors at 1 institution in 1 country.

Lei LiDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
E Neil G Marsh
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
HOW DO ENZYMES GENERATE AND CONTROL FREE RADICALSR01GM059227 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARSH, E NEIL · 1999 to 2007
$2.0M
NIGMS NIH HHS GM59227NIGMS NIH HHS R01 GM059227NIGMS NIH HHS R01 GM093088
6 · The paper itself

Abstract

Benzylsuccinate synthase catalyzes the first step in the anaerobic metabolism of toluene through an unusual reaction in which toluene is added to fumarate to produce (R)-benzylsuccinate. We have exploited the broad substrate range of the enzyme to demonstrate that the enzyme can catalyze the exchange of p-cresol with the benzyl portion of benzylsuccinate to form (4-hydroxybenzyl)-succinate, indicating that the reverse reaction (disproportionation of benzylsuccinate to toluene and fumarate) must have occurred. Even though the equilibrium constant for the reverse reaction is extremely unfavorable, Keq approximately 8 x 10-11 M at 4 degrees C, the enzyme catalyzes the reverse reaction at a rate only 250-fold slower than the forward reaction. Furthermore, using deuterium-labeled benzylsuccinate we observe partial exchange of deuterium with the solvent. This provides the first direct evidence that the migrating hydrogen is transferred to a labile site on the protein during catalysis, which is consistent with the participation of the proposed active-site cysteine residue in the mechanism of BSS.

Indexed as

Carbon-Carbon LyasesCatalysisChromatography, High Pressure LiquidFree RadicalsIsotopesMolecular StructureSubstrate Specificitybenzylsuccinate synthaseCarbon-Carbon LyasesFree RadicalsIsotopes

Identifiers

PMID17165757
PMCPMC2527060
OpenAlexW2007500196

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.