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Short-chain dehydrogenases/reductases (SDR)

H Jörnvall1, B Persson, M Krook

  • 1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.

Biochemistry
|May 9, 1995
PubMed
Summary

Short-chain dehydrogenases/reductases (SDR) are a diverse protein family with conserved catalytic residues and structural features. Comparative analysis reveals evolutionary relationships and aids in understanding enzyme function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Short-chain dehydrogenases/reductases (SDR) represent a large, diverse protein superfamily with over 57 characterized enzymes.
  • These enzymes exhibit low sequence identity (15-30%), suggesting ancient origins and significant divergence.
  • Additional SDR-related enzymes with extended chains and varied EC classes further expand the superfamily.

Purpose of the Study:

  • To investigate the conserved features and evolutionary relationships within the SDR superfamily.
  • To elucidate the catalytic mechanism and structural basis of SDR enzyme function.
  • To highlight the importance of comparative analysis in protein family research.

Main Methods:

  • Comparative sequence analysis to identify conserved residues and patterns.

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  • Review of existing biochemical and structural data, including X-ray crystallography.
  • Analysis of protein modification and mutagenesis studies.

    • Main Results:

    • Identified a strictly conserved tyrosine residue (Tyr 151) crucial for enzymatic function across the SDR superfamily.
    • A conserved lysine residue downstream of Tyr 151 also plays a role in catalysis.
    • A common GlyXXXGlyXGly motif in the N-terminal region facilitates coenzyme binding (NAD(H)/NADP(H)).
    • X-ray crystallography of two SDR enzymes revealed a conserved one-domain subunit structure with beta-strands and alpha-helices.
    • Most SDR enzymes function as dimers or tetramers, with subunit interactions mediated by specific alpha-helices.

    Conclusions:

    • The SDR superfamily exhibits remarkable structural and functional conservation despite sequence divergence.
    • A conserved catalytic dyad (Tyr-Lys) and coenzyme binding motif are key features.
    • Comparative studies are essential for uncovering hidden relationships and understanding enzyme mechanisms within large protein families.