A common structural motif in thiamin pyrophosphate‐binding enzymes

FEBS Letters

Hawkins, Christopher F.¹  Perham, Richard N.¹  Borges, Adolfo¹ 

[1] Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 IQW, England

关键词: Thiamin pyrophosphate;    Structural motif;    Sequence homology;    Pyruvate dehydrogenase complex;    Pyruvate decarboxylase;    Transketolase;    TPP;    thiamin pyrophosphate;   

DOI  :  10.1016/0014-5793(89)81064-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 βαβ 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.

【 授权许可】

Unknown