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 PDOC00329DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00329
Description
Three different enzymes - all pyridoxal-dependent decarboxylases - seem to share regions of sequence similarity [1,2,3,4], especially in the vicinity of the lysine residue which serves as the attachment site for the pyridoxal-phosphate (PLP) group. These enzymes are:
- Glutamate decarboxylase (EC 4.1.1.15) (GAD). Catalyzes the decarboxylation of glutamate into the neurotransmitter GABA (4-aminobutanoate).
- Histidine decarboxylase (EC 4.1.1.22) (HDC). Catalyzes the decarboxylation of histidine to histamine. There are two completely unrelated types of HDC: those that use PLP as a cofactor (found in Gram-negative bacteria and mammals), and those that contain a covalently bound pyruvoyl residue (found in Gram-positive bacteria).
- Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) (DDC), also known as L-dopa decarboxylase or tryptophan decarboxylase. DDC catalyzes the decarboxylation of tryptophan to tryptamine. It also acts on 5-hydroxy- tryptophan and dihydroxyphenylalanine (L-dopa).
- Tyrosine decarboxylase (EC 4.1.1.25) (TyrDC) which converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides.
- Cysteine sulfinic acid decarboxylase (EC 4.1.1.29).
- L-2,4-diaminobutyrate decarboxylase (EC 4.1.1.-) (DABA decarboxylase).
These enzymes are collectively known as group II decarboxylases [3,4].
Last update:April 2006 / Pattern revised.
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Technical section
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References
| 1 | Authors | Jackson F.R. |
| Title | Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous. | |
| Source | J. Mol. Evol. 31:325-329(1990). | |
| PubMed ID | 2124279 |
| 2 | Authors | Joseph D.R. Sullivan P.M. Wang Y.-M. Kozak C. Fenstermacher D.A. Behrendsen M.E. Zahnow C.A. |
| Title | Characterization and expression of the complementary DNA encoding rat histidine decarboxylase. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 87:733-737(1990). | |
| PubMed ID | 2300558 |
| 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 | Ishii S. Mizuguchi H. Nishino J. Hayashi H. Kagamiyama H. |
| Title | Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. | |
| Source | J. Biochem. 120:369-376(1996). | |
| PubMed ID | 8889823 |
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