Evidence map›Paper›PMID 26582199›Full record

ArticleThe Journal of biological chemistry2016

S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase.

João B Vicente, Henrique G Colaço, Paolo Sarti, Paula Leandro, Alessandro Giuffrè

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Intersection of HNeurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  3. Article
  4. Review
  5. A Metabolic Paradigm for Hydrogen Sulfide SignalingAntioxidants & redox signaling · 2023
    Review
  6. Review
  7. Review
  8. Review
  9. Structural perspectives on HCurrent opinion in structural biology · 2021
    Review
  10. Human Cystathionine γ-Lyase Is Inhibited byAntioxidants (Basel, Switzerland) · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Hydrogen Sulfide Metabolism and Signaling in the Tumor Microenvironment.Advances in experimental medicine and biology · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Chemical Biology of HChemical reviews · 2018
    Review
  20. Review
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

5 authors at 4 institutions in 2 countries.

João B VicenteFrom the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-156 Oeiras, Portugal, jvicente@itqb.unl.pt.
Henrique G Colaçothe Metabolism and Genetics Group, Research Institute for Medicines, Faculty of Pharmacy, University of Lisbon, 1649-003 Lisbon, Portugal.
Paolo Sartithe Department of Biochemical Sciences and Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, I-00185 Rome, Italy.
Paula Leandrothe Metabolism and Genetics Group, Research Institute for Medicines, Faculty of Pharmacy, University of Lisbon, 1649-003 Lisbon, Portugal, the Department of Biochemistry and Human Biology, Faculty of Pharmacy, University of Lisbon, 1640-003 Lisbon, Portugal, and.
Alessandro Giuffrèthe Institute of Molecular Biology and Pathology, National Research Council of Italy, I-00185 Rome, Italy alessandro.giuffre@uniroma1.it.
University of Lisbon · PTIstituto Pasteur · ITNational Research Council · ITUniversidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystathionine β-synthase (CBS) is a key enzyme in human (patho)physiology with a central role in hydrogen sulfide metabolism. The enzyme is composed of a pyridoxal 5'-phosphate-binding catalytic domain, flanked by the following two domains: a heme-binding N-terminal domain and a regulatory C-terminal domain binding S-adenosyl-l-methionine (AdoMet). CO or NO(•) binding at the ferrous heme negatively modulates the enzyme activity. Conversely, AdoMet binding stimulates CBS activity. Here, we provide experimental evidence for a functional communication between the two domains. We report that AdoMet binding significantly enhances CBS inhibition by CO. Consistently, we observed increased affinity (∼5-fold) and faster association (∼10-fold) of CO to the ferrous heme at physiological AdoMet concentrations. NO(•) binding to reduced CBS was also enhanced by AdoMet, although to a lesser extent (∼2-fold higher affinity) as compared with CO. Importantly, CO and NO(•) binding was unchanged by AdoMet in a truncated form of CBS lacking the C-terminal regulatory domain. These unprecedented observations demonstrate that CBS activation by AdoMet puzzlingly sensitizes the enzyme toward inhibition by exogenous ligands, like CO and NO(•). This further supports the notion that CBS regulation is a complex process, involving the concerted action of multiple physiologically relevant effectors.

Indexed as

Carbon MonoxideCystathionine beta-SynthaseHemeHumansKineticsMethionineNitric OxideOxidation-ReductionS-AdenosylmethionineCarbon MonoxideCystathionine beta-SynthaseHemeMethionineNitric OxideS-Adenosylmethionineallosteric regulationcarbon monoxidehemehydrogen sulfidenitric oxideS-adenosylmethioninesignal transduction

Identifiers

PMID26582199
PMCPMC4705378
OpenAlexW2176440103

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.