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PROSITE documentation PDOC00685 [for PROSITE entry PS00878] |
Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [1,2,3]. The second family consists of:
The above proteins, while most probably evolutionary related, do not share extensive regions of sequence similarities. We selected two of the conserved regions as signature patterns. The first pattern contains a conserved lysine residue which is known, in mouse ODC [4], to be the site of attachment of the pyridoxal-phosphate group. The second pattern contains a stretch of three consecutive glycine residues and has been proposed to be part of a substrate-binding region [5].
These enzymes are collectively known as group IV decarboxylases [3].
Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Bairoch A. |
Source | Unpublished observations (1993). |
2 | Authors | Martin C. Cami B. Yeh P. Stragier P. Parsot C. Patte J.-C. |
Source | Mol. Biol. Evol. 5:549-559(1988). |
3 | Authors | Sandmeier E. Hale T.I. Christen P. |
Title | Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. | |
Source | Eur. J. Biochem. 221:997-1002(1994). | |
PubMed ID | 8181483 |
4 | Authors | Poulin R. Lu L. Ackermann B. Bey P. Pegg A.E. |
Title | Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. | |
Source | J. Biol. Chem. 267:150-158(1992). | |
PubMed ID | 1730582 |
5 | Authors | Moore R.C. Boyle S.M. |
Title | Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. | |
Source | J. Bacteriol. 172:4631-4640(1990). | |
PubMed ID | 2198270 |