Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Alternative nitric oxide-producing substrates for NO synthases.

Daniel Mansuy1, Jean-Luc Boucher

  • 1UMR 8601-Université Paris 5, 75270 Paris Cedex 06, France. daniel.mansuy@univ-paris5.fr

Free Radical Biology & Medicine
|September 29, 2004
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Characterization of the Orphan Cytochrome P450 CYP135B1 from <i>Mycobacterium tuberculosis</i>: Involvement in Metabolism but Not in the Antibacterial Activity of the Antitubercular Drug SQ109.

ACS infectious diseases·2025
Same author

Inhibition of the Parkinson's Disease-Related Protein DJ-1 by Endogenous Neurotoxins of the 1,2,3,4-Tetrahydroisoquinoline Family.

ACS chemical neuroscience·2025
Same author

<i>S</i>-Ethyl-Isothiocitrullin-Based Dipeptides and 1,2,4-Oxadiazole Pseudo-Dipeptides: Solid Phase Synthesis and Evaluation as NO Synthase Inhibitors.

Molecules (Basel, Switzerland)·2023
Same author

Inhibition by pesticides of the DJ-1/Park7 protein related to Parkinson disease.

Toxicology·2023
Same author

Human Orphan Cytochrome P450 2U1 Catalyzes the ω-Hydroxylation of Leukotriene B<sub>4</sub>.

International journal of molecular sciences·2022
Same author

Unstability of cinnabarinic acid, an endogenous metabolite of tryptophan, under situations mimicking physiological conditions.

Biochimie·2022

Researchers explored various compounds as nitric oxide (NO) donors, finding that N-substituted N'-hydroxyguanidines and guanidines can produce NO. NOS II is more effective than NOS I and III in catalyzing this reaction with exogenous substrates.

Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Nitric oxide (NO) is a crucial signaling molecule in mammals, essential for vascular tone, neuronal communication, and immune responses.
  • NO biosynthesis occurs via the NO-synthase (NOS) enzymes, which catalyze the oxidation of L-arginine (L-Arg) to citrulline and NO.
  • Understanding NOS substrate specificity is key to developing NO-releasing therapeutics.

Purpose of the Study:

  • To investigate a range of synthetic compounds as potential substrates for NO production by NOS enzymes.
  • To evaluate the catalytic efficiency of these compounds in NO synthesis.
  • To compare the substrate preferences of different NOS isoforms (NOS I, II, and III).

Main Methods:

  • Synthesis of diverse guanidine and N-hydroxyguanidine derivatives.

Related Experiment Videos

  • Enzymatic assays using recombinant NOS isoforms to measure NO production.
  • Kinetic analysis (kcat, Km) to determine catalytic efficiency.

    • Main Results:

    • N-monosubstituted N itroguanidines and guanidines containing the NHC(NH2)=NH or NOH moiety were effective NO producers.
    • N-aryl and N-alkyl N itroguanidines showed significant NO production, with efficiency up to 50% of Nomega-hydroxy-L-arginine (NOHA).
    • NOS II demonstrated higher catalytic activity for exogenous guanidine and N-hydroxyguanidine oxidation compared to NOS I and III.

    Conclusions:

    • Specific N-substituted N itroguanidines and guanidines can serve as substrates for NO synthesis by NOS enzymes.
    • The size of the substituent on the guanidine moiety influences substrate recognition and catalytic efficiency.
    • NOS II exhibits distinct substrate preferences, offering potential for isoform-selective NO modulation.