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FEBS Lett. 1989 Sep 11;255(1):77-82.

A common structural motif in thiamin pyrophosphate-binding enzymes.

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1
Department of Biochemistry, University of Cambridge, England.

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.

PMID:
2792374
DOI:
10.1016/0014-5793(89)81064-6
[Indexed for MEDLINE]
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