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PROSITE documentation PDOC00329 |
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:
These enzymes are collectively known as group II decarboxylases [3,4].
Last update:April 2006 / Pattern revised.
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PROSITE method (with tools and information) covered by this documentation:
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 |