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000023567 0247_ $$2DOI$$a10.1074/jbc.M205699200
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000023567 084__ $$2WoS$$aBiochemistry & Molecular Biology
000023567 1001_ $$0P:(DE-HGF)0$$aPiotrowski, M.$$b0
000023567 245__ $$aPlant C-N-Hydrolases and the identification of a plant N-Carbamoylputrescine amidohydrolase involved in polyamine biosynthesis
000023567 260__ $$aBethesda, Md.$$bSoc.$$c2003
000023567 300__ $$a1708 - 1712
000023567 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000023567 440_0 $$03091$$aJournal of Biological Chemistry$$v278$$x0021-9258$$y3
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000023567 520__ $$aA nitrilase-like protein from Arabidopsis thaliana (NLP1) was expressed in Escherichia coli as a His(6)-tagged protein and purified to apparent homogeneity by Ni(2+)-chelate affinity chromatography. The purified enzyme showed N-carbamoylputrescine amidohydrolase activity, an enzyme involved in the biosynthesis of polyamines in plants and bacteria. N-carbamoylputrescine amidohydrolase activity was confirmed by identification of two of the three occurring products, namely putrescine and ammonia. In contrast, no enzymatic activity could be detected when applying various compounds including nitriles, amines, and amides as well as other N-carbamoyl compounds, indicating the specificity of the enzyme for N-carbamoylputrescine. Like the homologous beta-alanine synthases, NLP1 showed positive cooperativity toward its substrate. The native enzyme had a molecular mass of 279 kDa as shown by blue-native polyacrylamide gel electrophoresis, indicating a complex of eight monomers. Expression of the NLP1 gene was found in all organs investigated, but it was not induced upon osmotic stress, which is known to induce biosynthesis of putrescine. This is the first report of cloning and expression of a plant N-carbamoylputrescine amidohydrolase and the first time that N-carbamoylputrescine amidohydrolase activity of a recombinant protein could be shown in vitro. NLP1 is one of the two missing links in the arginine decarboxylase pathway of putrescine biosynthesis in higher plants.
000023567 536__ $$0G:(DE-Juel1)FUEK257$$2G:(DE-HGF)$$aChemie und Dynamik der Geo-Biosphäre$$cU01$$x0
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000023567 650_2 $$2MeSH$$aArabidopsis: enzymology
000023567 650_2 $$2MeSH$$aBiogenic Polyamines: biosynthesis
000023567 650_2 $$2MeSH$$aBlotting, Northern
000023567 650_2 $$2MeSH$$aElectrophoresis, Polyacrylamide Gel
000023567 650_2 $$2MeSH$$aMass Spectrometry
000023567 650_2 $$2MeSH$$aPhylogeny
000023567 650_2 $$2MeSH$$aUreohydrolases: chemistry
000023567 650_2 $$2MeSH$$aUreohydrolases: genetics
000023567 650_2 $$2MeSH$$aUreohydrolases: metabolism
000023567 650_7 $$00$$2NLM Chemicals$$aBiogenic Polyamines
000023567 650_7 $$0EC 3.5.3.-$$2NLM Chemicals$$aN-carbamoylputrescine hydrolase
000023567 650_7 $$0EC 3.5.3.-$$2NLM Chemicals$$aUreohydrolases
000023567 650_7 $$2WoSType$$aJ
000023567 7001_ $$0P:(DE-HGF)0$$aJanowitz, T.$$b1
000023567 7001_ $$0P:(DE-Juel1)VDB4417$$aKneifel, H.$$b2$$uFZJ
000023567 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M205699200$$gVol. 278, p. 1708 - 1712$$p1708 - 1712$$q278<1708 - 1712$$tThe @journal of biological chemistry$$v278$$x0021-9258$$y2003
000023567 8567_ $$uhttp://hdl.handle.net/2128/2663$$uhttp://dx.doi.org/10.1074/jbc.M205699200
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