PROSITE documentation PDOC00585Orn/Lys/Arg decarboxylases family 1 pyridoxal-phosphate attachment site
Description
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]. The first family consists of:
- Prokaryotic ornithine decarboxylase (EC 4.1.1.17) (ODC). ODC catalyzes the transformation of ornithine into putrescine.
- Prokaryotic lysine decarboxylase (EC 4.1.1.18) (LDC). LDC catalyzes the transformation of lysine into cadaverine.
- Escherichia coli biodegradative arginine decarboxylase (EC 4.1.1.19) (ADC). ADC catalyzes the transformation of arginine into agmatine.
- Bacillus subtilis hypothetical protein yaaO.
One of the regions of sequence similarity contains a conserved lysine residue which is known, in Escherichia coli LDC [3] and in ADC [4], to be the site of attachment of the pyridoxal-phosphate group. We have used this region as a signature pattern.
These enzymes are collectively known as group III decarboxylases [2].
Last update:November 1997 / Text revised.
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References
| 1 | Authors | Bairoch A. |
| Source | Unpublished observations (1993). |
| 2 | Authors | Sandmeier E. Hale T.I. Christen P. |
| Source | Eur. J. Biochem. 221:997-1002(1994). |
| 3 | Authors | Meng S.-Y. Bennett G.N. |
| Title | Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. | |
| Source | J. Bacteriol. 174:2659-2669(1992). | |
| PubMed ID | 1556085 |
| 4 | Authors | Stim K.P. Bennett G.N. |
| Title | Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli. | |
| Source | J. Bacteriol. 175:1221-1234(1993). | |
| PubMed ID | 8383109 |
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