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

Polyprenyl diphosphate synthases

K Ogura1, T Koyama, H Sagami

  • 1Institute for Chemical Reaction Science, Tohoku University, Sendai, Japan.

Sub-Cellular Biochemistry
|January 1, 1997
PubMed
Summary

Prenyltransferases exhibit diverse catalytic functions based on product chain length and stereochemistry. This study classifies these enzymes into four groups, highlighting unique cofactor and protein component requirements for different prenyl diphosphate syntheses.

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

International multicenter retrospective study on pleomorphic rhabdomyosarcoma (P-RMS), a PUSH platform study: outcome of primary localized disease.

ESMO open·2026
Same author

Low-grade fibromyxoid sarcoma and sclerosing epithelioid fibrosarcoma, outcome of advanced disease: retrospective study from the Ultra-Rare Sarcoma Working Group.

ESMO open·2024
Same author

Cepharanthine induces the proliferation of human dermal papilla cells and stimulates vascular endothelial growth factor expression through increased intracellular calcium mobilization and hypoxia-inducible factor activation.

Clinical and experimental dermatology·2020
Same author

A clinical comparison between dedifferentiated low-grade osteosarcoma and conventional osteosarcoma.

The bone & joint journal·2019
Same author

Burst intensification by singularity emitting radiation in multi-stream flows.

Scientific reports·2017
Same author

Scintillator-based transverse proton beam profiler for laser-plasma ion sources.

The Review of scientific instruments·2017

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Prenyltransferases catalyze essential reactions in isoprenoid biosynthesis.
  • The functional diversity of prenyltransferases is linked to product chain length and stereochemistry.

Purpose of the Study:

  • To classify prenyl diphosphate synthases based on their catalytic mechanisms and requirements.
  • To elucidate the distinct functional characteristics of enzymes synthesizing short-, medium-, and long-chain prenyl diphosphates.

Main Methods:

  • Enzyme classification based on reaction products and catalytic machinery.
  • Comparative analysis of cofactor and protein component requirements across different prenyl diphosphate synthases.

Main Results:

  • Prenyltransferases are categorized into four groups based on distinct functional modes.
  • Short-chain synthases require metal ions, medium-chain synthases involve dissociable protein components, long-chain synthases utilize carrier proteins, and Z-chain synthases require phospholipids.
  • Mammalian and bacterial classifications are similar, with mammalian cells featuring longer-chain Z-prenyl diphosphate synthases like dehydrodolichyl PP synthase.

Conclusions:

  • Prenyltransferase function is highly adaptable, with diverse mechanisms for product release and catalysis.
  • Dehydrodolichyl PP synthase is a key mammalian enzyme involved in glycoprotein biosynthesis and a target for future research.

Related Experiment Videos