Drosophila kelch motif is derived from a common enzyme fold

J Mol Biol. 1994 Mar 11;236(5):1277-82. doi: 10.1016/0022-2836(94)90056-6.


A systematic screening of sequence databases with a motif hitherto found only in animal and poxvirus proteins has revealed a trail leading back to prokaryotes. Fortuitously, an X-ray structure is available for one of the identified sequences and shows the fundamental fold to be a set of circularly arranged beta sheets. This structure may be very widely distributed throughout the biological world in sialidases and some other enzymes. In bacteria, a mobile noncatalytic domain is often associated with these same enzymes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Amino Acid Sequence*
  • Animals
  • Bacteria / enzymology
  • Biological Evolution
  • Drosophila / enzymology
  • Fungi / enzymology
  • Galactose Oxidase / chemistry*
  • Molecular Sequence Data
  • Neuraminidase / chemistry*
  • Protein Structure, Secondary
  • Repetitive Sequences, Nucleic Acid
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Viruses / enzymology


  • Alcohol Oxidoreductases
  • glyoxal oxidase
  • Galactose Oxidase
  • Neuraminidase