1996
DOI: 10.1016/0305-0491(95)02013-6
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Purification and characterisation of l-DOPA decarboxylase from pharate pupae of Ceratitis capitata. A comparison with the enzyme purified from the white prepupae

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Cited by 14 publications
(8 citation statements)
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“…In terms of substrate specificity, the DDC molecule purified from insects demonstrated a remarkably high affinity towards the decarboxylation of L-Dopa to dopamine (Fragoulis and Sekeris, 1975;Mappouras and Fragoulis, 1988;Bossinakou and Fragoulis, 1996). However, work by Mappouras et al (1990) in the normal human kidney has suggested that the enzyme is capable of also decarboxylating L-5-Hydroxytryptophan to serotonin, although the decarboxylation activity towards L-5-Hydroxytryptophan was found to be considerably lower than the one observed for L-Dopa (Mappouras et al, 1990).…”
Section: Functionmentioning
confidence: 95%
See 1 more Smart Citation
“…In terms of substrate specificity, the DDC molecule purified from insects demonstrated a remarkably high affinity towards the decarboxylation of L-Dopa to dopamine (Fragoulis and Sekeris, 1975;Mappouras and Fragoulis, 1988;Bossinakou and Fragoulis, 1996). However, work by Mappouras et al (1990) in the normal human kidney has suggested that the enzyme is capable of also decarboxylating L-5-Hydroxytryptophan to serotonin, although the decarboxylation activity towards L-5-Hydroxytryptophan was found to be considerably lower than the one observed for L-Dopa (Mappouras et al, 1990).…”
Section: Functionmentioning
confidence: 95%
“…The DDC enzyme (EC 4.1.1.28) was initially purified and characterized from pig kidney (Christenson et al, 1970) as well as from the insects Calliphora vicina (Fragoulis and Sekeris, 1975) and Ceratitis capitata (Mappouras and Fragoulis, 1988;Bossinakou and Fragoulis, 1996). DDC is a homodimer of 100-110 kDa, with a subunit molecular mass of 50-55 kDa (Voltattorni et al, 1979;Mappouras et al, 1990;Bossinakou and Fragoulis, 1996). The full-length protein molecule consists of 480 amino acids (Ichinose et al, 1989).…”
Section: Descriptionmentioning
confidence: 99%
“…LDopa decarboxylase is considered as a cytosolic enzyme, whose membrane-associated active form has been detected in the mammalian brain [44]. DDC has been purified and characterized from a variety of mammalian peripheral organs [45][46][47][48], as well as from developing insects [49][50][51][52]. However, the physiological role of the peripheral enzyme is not adequately determined yet.…”
Section: Introductionmentioning
confidence: 99%
“…Συγκεκριμένα, τα δισθενή κατιόντα Cu 2+ , Hg 2+ , και Fe 2+ επιδρούν ανασταλτικά στην ενεργότητα του ενζύμου που απομονώνεται από τις ώριμες νύμφες του εντόμου Ceratitis capitata, ενώ τα κατιόντα Zn 2+ και Al 3+ την αναστέλλουν πλήρως (Bossinakou and Fragoulis, 1996). Ιδιαίτερα ισχυρή ανασταλτική επίδραση στην ενεργότητα της ανθρώπινης DDC ασκούν τα δισθενή κατιόντα Cu 2+ , Hg 2+ , και Zn 2+ .…”
Section: εντόπιση της L-dopa αποκαρβοξυλάσης σε ιστούς θηλαστικώνunclassified