A common structural motif in thiamin pyrophosphate-binding enzymes

FEBS Lett. 1989 Sep 11;255(1):77-82. doi: 10.1016/0014-5793(89)81064-6.

Abstract

The amino acid sequences of a wide range of enzymes that utilize thiamin pyrophosphate (TPP) as cofactor have been compared. A common sequence motif approximately 30 residues in length was detected, beginning with the highly conserved sequence -GDG- and concluding with the highly conserved sequence -NN-. Secondary structure predictions suggest that the motif may adopt a beta alpha beta fold. The same motif was recognised in the primary structure of a protein deduced from the DNA sequence of a hitherto unassigned open reading frame of Rhodobacter capsulata. This putative protein exhibits additional homology with some but not all of the TPP-binding enzymes.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carboxy-Lyases / genetics*
  • Carrier Proteins / genetics
  • Genes*
  • Humans
  • Molecular Sequence Data
  • Pyruvate Decarboxylase / genetics*
  • Pyruvate Dehydrogenase Complex / genetics*
  • Sequence Homology, Nucleic Acid
  • Software
  • Thiamine Pyrophosphate* / physiology
  • Transketolase / genetics*

Substances

  • Carrier Proteins
  • Pyruvate Dehydrogenase Complex
  • Transketolase
  • Carboxy-Lyases
  • Pyruvate Decarboxylase
  • Thiamine Pyrophosphate