type	Journal Article
authors	Sumi, C.; Ichinose, H.; Nagatsu, T.
title	Characterization of recombinant human aromatic L-amino acid decarboxylase expressed in COS cells
journal	J Neurochem
Activity	4.1.1.28
ui	90347447
year	(1990)
volume	55
number	3
pages	1075-8.
keywords	5-Hydroxytryptophan/metabolism
abstract	The expression vector containing the full-length cDNA of human aromatic L-amino acid decarboxylase (EC 4.1.1.28) was transfected in COS cells by a modified calcium phosphate coprecipitation method. The cells transfected with plasmids that had a true direction of the cDNA gave a major immunoreactive band at 50 kDa. This expressed enzyme catalyzed the decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA), L-5- hydroxytryptophan (L-5-HTP) and L-threo-3,4-dihydroxyphenylserine. The optimal pH of the enzyme activity with L-DOPA as a substrate was 6.5, whereas the enzyme had a broad pH optimum when L-5-HTP was used as a substrate. Addition of pyridoxal phosphate to the incubation mixture greatly enhanced the activity for both L-DOPA and L-5-HTP.
last changed	2002/11/12 16:17