A common structural motif in thiamin pyrophosphate-binding enzymes.
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.
Hawkins
C F
CF
Department of Biochemistry, University of Cambridge, England.
Borges
A
A
Perham
R N
RN
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002262:Carboxy-Lyases / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics; D005796:Genes; D006801:Humans; D008969:Molecular Sequence Data; D011767:Pyruvate Decarboxylase / Q000235:genetics*; D011768:Pyruvate Dehydrogenase Complex / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D012984:Software; D013835:Thiamine Pyrophosphate / Q000502:physiology; D014174:Transketolase / Q000235:genetics*
D002352:Carrier Proteins; D011768:Pyruvate Dehydrogenase Complex; D014174:Transketolase; D002262:Carboxy-Lyases; D011767:Pyruvate Decarboxylase; D013835:Thiamine Pyrophosphate