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

Conservation, evolution, and specificity in cellular control by protein phosphorylation

H W Hofer1

  • 1University of Konstanz, Faculty of Biology, Germany.

Experientia
|May 15, 1996
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

Reduction of atherosclerotic nanoplaque formation and size by Ginkgo biloba (EGb 761) in cardiovascular high-risk patients.

Atherosclerosis·2007
Same author

Protein tyrosine phosphatase 1B is located with glucagon vesicles, and its concentration is inversely correlated with the rate of glucagon secretion of INR1G9 cells.

The Journal of endocrinology·2004
Same author

A non-receptor-type protein phosphotyrosine phosphatase is enriched in secretory vesicles of glucagon - and pancreatic polypeptide - secreting cells of the endocrine pancreas.

Histochemistry and cell biology·1999
Same author

Ascaris suum: protein phosphotyrosine phosphatases in oocytes and developing stages.

Experimental parasitology·1998
Same author

Vascular smooth muscle, a multiply feedback-coupled system of high versatility, modulation and cell-signaling variability.

International journal of microcirculation, clinical and experimental·1998
Same author

Activation by phosphorylation of phosphofructokinase from the annelid Lumbricus terrestris and comparison of phosphorylated sites in invertebrate phosphofructokinases.

The Biochemical journal·1996

Phosphofructokinase in the parasitic nematode Ascaris lumbricoides is controlled by phosphorylation. Unique protein kinase and specific phosphatases regulate this glycolytic enzyme, differing from mammalian counterparts.

Area of Science:

  • Biochemistry
  • Parasitology
  • Enzymology

Background:

  • Phosphofructokinase is a key glycolytic enzyme.
  • Regulation of phosphofructokinase activity is crucial for metabolic control.
  • Parasitic nematodes possess unique biochemical pathways.

Purpose of the Study:

  • To investigate the regulation of phosphofructokinase in Ascaris lumbricoides.
  • To characterize the protein kinase and phosphatases involved in its phosphorylation.
  • To understand the structural basis for substrate specificity differences.

Main Methods:

  • Enzyme purification and characterization.
  • Kinase and phosphatase assays.
  • Structural analysis of the protein kinase.

Related Experiment Videos

Main Results:

  • Ascaris lumbricoides phosphofructokinase is regulated by reversible phosphorylation.
  • An atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase phosphorylates the enzyme.
  • The protein kinase exhibits substrate specificity distinct from mammalian enzymes due to structural features.
  • Phosphatases involved are specific to glycolysis and differ from those in glycogenolysis.

Conclusions:

  • The regulation of phosphofructokinase in Ascaris lumbricoides involves unique enzymatic machinery.
  • Structural differences in the protein kinase explain its substrate specificity.
  • Specialized phosphatases highlight distinct regulatory mechanisms in parasitic nematode glycolysis.