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Related Experiment Videos

The TIM-barrel fold: a versatile framework for efficient enzymes.

R K Wierenga1

  • 1Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, Oulu, Finland. rik.wierenga@oulu.fi

FEBS Letters
|March 21, 2001
PubMed
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Triosephosphate isomerase (TIM)-barrel enzymes showcase scaffold versatility across 15 families. Structural and sequence analyses reveal evolutionary links and common properties among these enzymes.

Area of Science:

  • Biochemistry and structural biology
  • Enzymology
  • Evolutionary biology

Background:

  • The triosephosphate isomerase (TIM)-barrel is a prevalent protein scaffold.
  • This structural motif is utilized by at least 15 distinct enzyme families.
  • The active site is consistently located at the C-terminal end of the eight parallel beta-strands.

Purpose of the Study:

  • To highlight the functional versatility of the TIM-barrel scaffold.
  • To explore the evolutionary relationships between different TIM-barrel enzyme families.
  • To discuss common structural characteristics shared by TIM-barrel enzymes.

Main Methods:

  • Comparative analysis of enzyme sequences.
  • Structural comparison of TIM-barrel enzymes.

Related Experiment Videos

  • Literature review of recent studies.

    • Main Results:

    • Demonstration of the remarkable versatility of the TIM-barrel scaffold.
    • Identification of at least 15 enzyme families employing this framework.
    • Evidence suggesting evolutionary relatedness among many TIM-barrel enzymes.
    • Discussion of shared structural properties.

    Conclusions:

    • The TIM-barrel scaffold is a highly versatile and evolutionarily conserved structural framework.
    • Understanding the common properties of TIM-barrel enzymes can provide insights into enzyme function and evolution.