Abstract
cDNA encoding serine Carboxypeptidase gene of Matricaria chamomilla was cloned by reverse transcription-polymerase chain reaction and rapid amplification of cDNA end techniques. The cloned cDNA contained an open reading frame consisting of 501 amino acids, which had two active site motifs of serine Carboxypeptidase and high homology with other plant carboxypeptidases. The M. chamomilla Carboxypeptidase was found to have leucine zipper structure at the N terminal region, suggesting that this enzyme functions at dimer form. Nine N-myristoylation sites in the enzyme let us anticipate that this enzyme localizes at a membrane or lipid layer.
