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

The structural basis for pyrophosphatase catalysis

P Heikinheimo1, J Lehtonen, A Baykov

  • 1Turku Centre for Biotechnology, Finland.

Structure (London, England : 1993)
|December 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

A novel approach to cervical dilation for second-trimester dilation and evacuation in a myomatous uterus.

Contraception·2025
Same author

Evaluating the prospective utility of pharmacogenetics reporting among Canadian Armed Forces personnel receiving pharmacotherapy: a preliminary assessment towards precision psychiatric care.

BMJ military health·2023
Same author

A phase II open-label trial of avelumab plus axitinib in previously treated non-small-cell lung cancer or treatment-naïve, cisplatin-ineligible urothelial cancer.

ESMO open·2023
Same author

Developing a platform for Fresnel diffractive radiography with 1 μm spatial resolution at the National Ignition Facility.

The Review of scientific instruments·2023
Same author

UPPER ARM CONTOURING - A NARRATIVE REVIEW.

Georgian medical news·2023
Same author

PIGMENTED NODULAR CYSTIC HIDRADENOMA OF THE ANKLE.

Georgian medical news·2021
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

High-resolution structures reveal yeast inorganic pyrophosphatase (PPase) uses a three-metal ion mechanism for catalysis. This finding clarifies phosphorus metabolism and phosphoryl transfer mechanisms, highlighting the enzyme

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Soluble inorganic pyrophosphatase (PPase) is crucial for phosphorus metabolism, catalyzing inorganic pyrophosphate hydrolysis.
  • Enzyme activity depends on divalent metal ions, affecting substrate and enzyme pKas.
  • Understanding PPase catalysis is vital for biological phosphoryl transfer mechanisms and divalent cation roles.

Purpose of the Study:

  • To elucidate the catalytic mechanism of yeast inorganic pyrophosphatase (PPase).
  • To obtain high-resolution structural data of PPase in complex with metal ions and products.
  • To develop a structure-based model for PPase-catalyzed hydrolysis.

Main Methods:

  • X-ray crystallography was used to determine the high-resolution structures of yeast PPase.

Related Experiment Videos

  • Structures were solved at 2.2 and 2.0 Å resolution.
  • Complexes with activating metal ions and the product (MnPi)2 were analyzed.

    • Main Results:

    • Two high-resolution structures of yeast PPase were determined.
    • One structure revealed activating metal ions, while the other contained the product (MnPi)2.
    • The product-bound structure showed extensive hydrogen bond and metal ion interactions, including a phosphate bound to four Mn2+ ions and a bridging hydroxide ion.

    Conclusions:

    • A structure-based model proposes a hydroxide ion as the nucleophile, analogous to other metalloenzymes.
    • A third metal ion likely acts as a general acid, coordinating a water molecule.
    • The proposed "three-metal ion" mechanism, with extensive Lewis acid coordination, differs from other phosphoryl transfer enzymes.