The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
A common structural motif in thiamin pyrophosphate‐binding enzymes
Open accessAbstract
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.
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Cites
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[47] Establishing homologies in protein sequences
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Cited by
The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
de Kok, A., Hengeveld, A. F., Martin, A., & Westphal, A. H. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00079-x · Cited by 174
Metadata
- Authors
- Hawkins, C. F., Borges, A., & Perham, R. N.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1989-09-11
- Volume
- 255
- Issue
- 1
- Pages
- 77-82
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1996726147
- Cited by
- 317
- References
- 20
- FWCI
- 7.07
- Type
- journal article
- Language
- en
- Open access
- bronze
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