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. doi: 10.1016/0006-291x(89)91772-5.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenal Gland Neoplasms / enzymology*
  • Adrenal Gland Neoplasms / genetics
  • Amino Acid Sequence
  • Animals
  • Aromatic-L-Amino-Acid Decarboxylases / genetics*
  • Base Sequence
  • Cloning, Molecular*
  • DNA, Neoplasm / genetics*
  • DNA, Neoplasm / isolation & purification
  • Drosophila / enzymology
  • Drosophila / genetics
  • Gene Library
  • Genes*
  • Humans
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • Pheochromocytoma / enzymology*
  • Pheochromocytoma / genetics
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • DNA, Neoplasm
  • Aromatic-L-Amino-Acid Decarboxylases