PR00800

YHDCRBOXLASE

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameYHDCRBOXLASE

Description
Imported from IPR010977

A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group
[1, 2]
. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase), which catalyses the decarboxylation of tryptophan to tryptamine
[3]
; tyrosine decarboxylase, which converts tyrosine into tyramine; and histidine decarboxylase, which catalyses the decarboxylation of histidine to histamine
[4]
. These enzymes belong to the group II decarboxylases
[1, 3]
.

References
Imported from IPR010977

1.Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. Sandmeier E, Hale TI, Christen P. Eur. J. Biochem. 221, 997-1002, (1994). View articlePMID: 8181483

2.Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous. Jackson FR. J. Mol. Evol. 31, 325-9, (1990). View articlePMID: 2124279

3.Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. Ishii S, Mizuguchi H, Nishino J, Hayashi H, Kagamiyama H. J. Biochem. 120, 369-76, (1996). View articlePMID: 8889823

4.Characterization and expression of the complementary DNA encoding rat histidine decarboxylase. Joseph DR, Sullivan PM, Wang YM, Kozak C, Fenstermacher DA, Behrendsen ME, Zahnow CA. Proc. Natl. Acad. Sci. U.S.A. 87, 733-7, (1990). View articlePMID: 2300558

Supplementary References

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