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

S-adenosylmethionine-dependent enzyme activation.

J W Kozarich1

  • 1Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.

Biofactors (Oxford, England)
|July 1, 1988
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

Inhibition and structure-activity studies of methionine hydroxamic acid derivatives with bacterial peptide deformylase.

Bioorganic chemistry·2005
Same author

Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis.

Biochimica et biophysica acta·2001
Same author

Inactivation of pyruvate formate-lyase by dioxygen: defining the mechanistic interplay of glycine 734 and cysteine 419 by rapid freeze-quench EPR.

Biochemistry·2001
Same author

Inhibition of bacterial peptide deformylase by biaryl acid analogs.

Archives of biochemistry and biophysics·2000
Same author

Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.

Structure (London, England : 1993)·1999
Same author

Purification and crystallization of a proteolytic fragment of Escherichia coli pyruvate formate-lyase.

Acta crystallographica. Section D, Biological crystallography·1999

S-Adenosylmethionine (SAM) activates enzymes through cleavage, forming active enzyme complexes. This process involves radical generation or methylation, crucial for biological functions.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • S-Adenosylmethionine (SAM) is a key biological methyl donor.
  • SAM-dependent enzymes play vital roles in various metabolic pathways.
  • Understanding enzyme activation mechanisms is crucial for biochemical research.

Purpose of the Study:

  • To discuss the activation mechanisms of three SAM-dependent enzymes.
  • To categorize the chemical processes involved in SAM-mediated enzyme activation.
  • To highlight the formation of catalytically active enzyme species upon SAM cleavage.

Main Methods:

  • Literature review of SAM-dependent enzyme mechanisms.
  • Analysis of biochemical pathways involving pyruvate formate-lyase, lysine 2,3-aminomutase, and methionine synthase.

Related Experiment Videos

  • Comparative study of radical and methylation chemistries in enzyme activation.

    • Main Results:

    • SAM cleavage consistently yields catalytically active enzymes.
    • Activation chemistry is categorized into three distinct classes.
    • Pyruvate formate-lyase activation involves essential enzyme radical generation.
    • Lysine 2,3-aminomutase activation forms a 5'-deoxyadenosyl radical.
    • Methionine synthase activation involves reductive methylation to form methylcobalamin.

    Conclusions:

    • SAM-dependent enzyme activation is diverse, involving distinct chemical strategies.
    • Radical intermediates and methylcobalamin formation are key outcomes of SAM cleavage.
    • These mechanisms underscore the versatility of SAM in biological catalysis.