In molecular biology, group II pyridoxal-dependent decarboxylases are family of enzymes including aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase) EC 4.1.1.28, which catalyses the decarboxylation of tryptophan to tryptamine, tyrosine decarboxylase EC 4.1.1.25, which converts tyrosine into tyramine and histidine decarboxylase EC 4.1.1.22, which catalyses the decarboxylation of histidine to histamine.[1][2]
| Pyridoxal-dependent decarboxylase conserved domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the murine class ii allele i-a(g7) complexed with the glutamic acid decarboxylase (gad65) peptide 207-220 | |||||||||
| Identifiers | |||||||||
| Symbol | Pyridoxal_deC | ||||||||
| Pfam | PF00282 | ||||||||
| Pfam clan | CL0061 | ||||||||
| InterPro | IPR002129 | ||||||||
| PROSITE | PDOC00329 | ||||||||
| SCOP2 | 1js3 / SCOPe / SUPFAM | ||||||||
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Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group II includes glutamate, histidine, tyrosine, and aromatic-L-amino-acid decarboxylases.[3]
See also
editReferences
edit- ^ Ishii S, Mizuguchi H, Nishino J, Hayashi H, Kagamiyama H (August 1996). "Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis". J. Biochem. 120 (2): 369–76. doi:10.1093/oxfordjournals.jbchem.a021422. PMID 8889823.
- ^ Joseph DR, Sullivan PM, Wang YM, Kozak C, Fenstermacher DA, Behrendsen ME, Zahnow CA (January 1990). "Characterization and expression of the complementary DNA encoding rat histidine decarboxylase". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 733–7. Bibcode:1990PNAS...87..733J. doi:10.1073/pnas.87.2.733. PMC 53340. PMID 2300558.
- ^ Sandmeier E, Hale TI, Christen P (May 1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases". Eur. J. Biochem. 221 (3): 997–1002. doi:10.1111/j.1432-1033.1994.tb18816.x. PMID 8181483.