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| PROSITE documentation PDOC00329 |
DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site
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.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| DDC_GAD_HDC_YDC, PS00392; DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site (PATTERN) |
| Consensus pattern: |
S-[LIVMFYW]-x-{KG}-x(3)-K-[LIVMFYWGH]-[LIVMFYWG]-x-{R}-x-[LIVMFYW]-{V}-[CA]-x(2)-[LIVMFYWQ]-{K}-x-[RK]
K is the pyridoxal-P attachment site |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for a probable Caenorhabditis elegans DDC and for Petunia GAD |
| Other sequence(s) detected in Swiss-Prot: |
5 |
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| Matching PDB structures:
1JS3 1JS6 1PMM 1PMO ... [ALL] |
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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