Go toArchive
Browse byFacets
Bookbag ( 0 )
'Spinacia oleracea' in keywords
Results  3 Items
Sorted by   
Section
Publication Year
1985 (2)
1981 (1)
1Author    Coralie Wink, Thom As, H. Artm AnnRequires cookie*
 Title    Properties and Subcellular Localization of L-Alanine: Aldehyde Aminotransferase: Concept of an Ubiquitous Plant Enzyme Involved in Secondary Metabolism  
 Abstract    L-Alanine: aldehyde aminotransferase occurs ubiquitously in higher plants. The enzyme catalyzes the reaction: L-alanine + monoaldehyde -> monoamine + pyruvate; it is responsible for the formation of aliphatic plant amines and involved in the biosynthesis o f hemlock alkaloids as shown by Roberts. A continuous coupled photometric test was developed to determine the low activities of the transaminase. The enzyme from the "amine-free" plant Spinacia oleracea was purified 77-fold and separated from other aminotransferases. A comparison of the Spinacia enzyme with that isolated from spadix-appendices o f the amine-producing Arum maculatum during anthesis revealed very similar characteristics in pH-dependence, ATm-values for alanine and aliphatic aldehydes, and inhibition by 2-oxoacids. In contrast to the Spinacia enzyme the Arum aminotransferase is rapidly inactivated in the absence o f pyridoxal-5'-phosphate. The enzymes o f S. oleracea, A. maculatum and Mercurialis perennis are localized in mitochondria, but not in chloroplasts or peroxisomes. The results are discussed in relation to the function o f alanine: aldehyde aminotransferase in secondary metabolism. It is suggested that some enzymes may be expressed in plants at low levels, even in the absence o f any metabolic function. 
  Reference    Z. Naturforsch. 36c, 625 (1981); received April 13 1981 
  Published    1981 
  Keywords    Spinacia oleracea, Arum maculatum, Alanine: Aldehyde Aminotransferase, Amine-Biosynthesis, Subcellular Localization, Mitochondria 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0625.pdf 
 Identifier    ZNC-1981-36c-0625 
 Volume    36 
2Author    Bodo LiedvogelRequires cookie*
 Title    Acetate Concentration and Chloroplast Pyruvate Dehydrogenase Complex in Spinacia oleracea Leaf Cells  
 Abstract    Acetate concentration in spinach (Spinacia oleracea L.) leaf tissue has been determined by direct m easurement in a leaf extract to oe 70 |xm or less. Additional evidence for such low acetate levels came from isotope dilution experiments where the [ l -14C]acetate incorporation into fatty acids was assayed using purified chloroplasts in the presence o f tissue extracts. Pyruvate dehydrogenase complex activity was shown to be present in spinach chloroplasts and was determined by a newly developed acetyl coenzym e A trapping system (100 nmol acetyl CoA formed per mg chloroplast protein per h). The problem s o f acetyl CoA synthesis in both compart­ ments, chloroplasts and cytoplasm, are discussed in this context. 
  Reference    Z. Naturforsch. 40c, 182 (1985); received D ecem ber 6 1984 
  Published    1985 
  Keywords    Spinacia oleracea, Acetate Concentration, Isotope D ilution, Chloroplast Pyruvate Dehydrogenase Complex, Acetyl Coenzyme A Assay 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0182.pdf 
 Identifier    ZNC-1985-40c-0182 
 Volume    40 
3Author    H. Om Eyer, D. S. Chulze-Siebert, G. SchultzRequires cookie*
 Title    On the Specificity o f the Herbicide Chlorsulfuron in Intact Spinach Chloroplasts  
 Abstract    In vitro incubation of intact spinach chloroplasts with 1 mM Pyruvate was used to study the specificity of action of the herbicide Chlorsulfuron on the synthesis of valine, alanine and fatty acids. As a result, increasing concentra­ tions of the herbicide strongly inhibited valine synthesis while fatty acid synthesis via pyruvate dehydrogenase com­ plex (PDC) and alanine formation by transamination reac­ tion was promoted. 
  Reference    Z. Naturforsch. 40c, 917—918 (1985); received September 27 1985 
  Published    1985 
  Keywords    Acetolactate Synthase, Chlorsulfuron, Fatty Acid Synthe­ sis, Pyruvate Dehydrogenase Complex, Spinacia oleracea 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0917_n.pdf 
 Identifier    ZNC-1985-40c-0917_n 
 Volume    40