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B6db references: 14738999

type Journal Article
authors Zhu, MY.; Iyo, A.; Piletz, J.E.; Regunathan, S.
title Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine
journal Biochim Biophys Acta
Activity odcp
sel selected
ui 14738999
year (2004)
volume 1670
number 2
pages 156-64
abstract Agmatine, an amine formed by decarboxylation of L-arginine by arginine decarboxylase (ADC), has been recently discovered in mammalian brain and other tissues. While the cloning and sequencing of ADC from plant and bacteria have been reported extensively, the structure of mammalian enzyme is not known. Using homology screening approach, we have identified a human cDNA clone that exhibits ADC activity when expressed in COS-7 cells. The cDNA and deduced amino acid sequence of this human ADC clone is distinct from ADC of other forms. Human ADC is a 460-amino acid protein that shows about 48% identity to mammalian ornithine decarboxylase (ODC) but has no ODC activity. While naive COS-7 cells do not make agmatine, these cells are able to produce agmatine, as measured by HPLC, when transfected with ADC cDNA. Northern blot analysis using the cDNA probe indicated the expression of ADC message in selective human brain regions and other human tissues.
last changed 2009/01/08 15:19

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