Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase.
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Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T
Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase.
Biochem Biophys Res Commun. 1989 Nov 15;164(3):1024-30.
- PubMed ID
- 2590185 [ View in PubMed]
- Abstract
The nucleotide sequence of a cDNA clone that includes the entire coding region of human aromatic L-amino acid decarboxylase gene is presented. A human pheochromocytoma cDNA library was screened using an oligonucleotide probe which corresponded to a partial amino acid sequence of the enzyme purified from the human pheochromocytoma. The isolated cDNA clone encoded a protein of 480 amino acids with a calculated molecular mass of 53.9 kDa. The amino acid sequence Asn-Phe-Asn-Pro-His-Lys-Trp around a possible cofactor (pyridoxal phosphate) binding site is identical in human, Drosophila, and pig enzymes.