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'Tyrosine' in keywords
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1992 (1)
1991 (1)
1Author    Hiroshi Hirano, M. Asaaki Sakuta, Atsushi Kom, Am IneRequires cookie*
 Title    Inhibition by Cytokinin of the Accumulation of Betacyanin in Suspension Cultures of Phytolacca americana  
 Abstract    The accumulation o f betacyanin was reduced by the addition o f various cytokinins to sus­ pension cultures o f Phytolacca americana. The decrease in the accumulation o f betacyanin was overcome by exogenously supplied tyrosine which is a precursor o f betacyanin. Benzylamino-purine (BAP) decreased the level o f free tyrosine in the cells. Feeding experiments using labeled tyrosine revealed that BAP reduced the incorporation o f labeled tyrosine into betacyanins (to about 50% o f the control rate). These results suggest that both the availability o f tyrosine and the biosynthetic activity o f the pathway from tyrosine to the betacyanins are involved in the inhibition o f the accumulation o f betacyanins by cytokinins in P hytolacca americana cells. 
  Reference    Z. Naturforsch. 47c, 705 (1992); received June 29/A ugust 17 1992 
  Published    1992 
  Keywords    Betacyanin, Cytokinin, Phytolacca americana, Suspension Culture, Tyrosine 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0705.pdf 
 Identifier    ZNC-1992-47c-0705 
 Volume    47 
2Author    Bengt Svensson, Imre Vass, Stenbjörn StyringRequires cookie*
 Title    Sequence Analysis of the D 1 and D 2 Reaction Center Proteins of Photosystem II  
 Abstract    A com pilation o f 38 sequences for the D1 and 15 sequences for the D 2 reaction center pro­ teins o f photosystem II is presented. The sequences have been compared and a similarity index that takes into account the degree o f conservation and the quality o f the changes in each posi­ tion has been calculated. The similarity index is used to identify and describe functionally im­ portant domains in the D 1 /D 2 heterodimer. Comparative hydropathy plot are presented for the aminoacid sidechains that constitute the binding domain o f the tyrosine radicals, Tyrz and TyrD, in photosystem II. The structure around Tyrz is more hydrophilic than the structure around TyrD. The hydrophilic residues are clustered in the part o f the binding pocket for Tyrz that is turned towards the lumenal side o f the thylakoid membrane. M ost prominent is the presence o f two conserved carboxylic am inoacids, D l-A sp 170 and D l-G lu 189. Their respec­ tive carboxyl-groups com e close in space and are proposed to constitute a metal binding site together with D l-G ln 165. The distance between the proposed metal binding site and the cen­ ter o f the ring o f Tyrz is approximately 7Ä . The cavity that constitutes the binding site for TyrD is com posed o f residues from the D 2 protein. Its character is more hydrophobic than the Tyrz site and the environment around TyrD lacks the cluster o f putative metal binding side­ chains. 
  Reference    Z. Naturforsch. 46c, 765 (1991); received March 13 1991 
  Published    1991 
  Keywords    Photosystem II, D1 Protein, D 2 Protein, Tyrosine, M anganese, Reaction Center 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0765.pdf 
 Identifier    ZNC-1991-46c-0765 
 Volume    46