We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00585Orn/Lys/Arg decarboxylases family 1 pyridoxal-phosphate attachment site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00585
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| Source | Unpublished observations (1993).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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