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Related Experiment Videos

The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations.

Domenico Bordo1, Peer Bork

  • 1National Cancer Research Institute, c/o Advanced Biotechnology Center, Genova, Italy. domenico@alcor.ge.infm.it

EMBO Reports
|August 2, 2002
PubMed
Summary

Rhodanese domains are versatile sulfur carriers involved in metabolic pathways. This review analyzes the rhodanese/Cdc25 phosphatase superfamily, suggesting a common evolutionary origin and a role for active-site loops in substrate specificity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Rhodanese domains are widespread structural motifs found across all three major evolutionary phyla.
  • These domains function as versatile sulfur carriers, adapting to diverse metabolic and regulatory pathways requiring reactive sulfane sulfur.
  • Recent findings link rhodanese domains to the catalytic subunit of Cdc25 phosphatase enzymes, suggesting a shared evolutionary ancestry.

Purpose of the Study:

  • To review and analyze the rhodanese/Cdc25 phosphatase superfamily.
  • To explore the functional versatility and evolutionary relationships of rhodanese domains.
  • To discuss the potential roles of active-site loops and inactive domains in enzyme function and regulation.

Main Methods:

  • Literature review and analysis of existing research on rhodanese domains and Cdc25 phosphatases.

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  • Comparative structural and evolutionary analysis of the rhodanese/Cdc25 phosphatase superfamily.
  • Examination of reported functional roles and potential substrate interactions.

    • Main Results:

    • Rhodanese domains are integral components in various biological processes, acting as sulfur carriers.
    • A structural and likely evolutionary relationship exists between rhodanese domains and Cdc25 phosphatase catalytic subunits.
    • The amino acid composition of the active-site loop appears crucial for substrate recognition and specificity.
    • Catalytically inactive rhodanese modules may play regulatory roles, potentially in signaling pathways.

    Conclusions:

    • The rhodanese/Cdc25 phosphatase superfamily represents a conserved protein family with diverse functions.
    • While specific substrates remain elusive, active-site loop variations dictate substrate specificity.
    • Inactive rhodanese domains likely possess regulatory functions, highlighting their multifaceted biological importance.