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'ATP Sulfurylase' in keywords
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1992 (1)
1977 (1)
1Author    Jens-Dirk Schwerin, Brigitte DepkaRequires cookie*
 Title    Assimilatory Sulfate Reduction by Chloroplasts: The Regulatory Influence of Adenosine-mono-and Adenosine-diphosphate  
 Abstract    The first three enzymatic steps of assimilatory sulfate reduction in chloroplasts of higher plants have been investigated with emphasis on the influence of adenosine-mono-and -diphosphate upon the formation of APS, PAPS and bound sulfite. The data show that the activation process is governed by the energy charge of the chloroplast. The regulatory step is localized at the ATP-sulfurylase reaction. It was found that this enzyme is inhibited by low concentrations of AMP and ADP, with apparent KjAMP = L8mM and K;aDV = 0 .5 mM for the chloroplast preparations. The isolated purified ATP-sulfurylase is inhibited by the nucleotides accordingly, with £ * A M P = 0 .2 m M and X j A D P = 0 .4 m M . The results are interpreted as a regulatory mechanism for the complete process of assimilatory sulfate reduction in the chloro­ plast. 
  Reference    (Z. Naturforsch. 32c, 792 [1977]; received August 29 1977) 
  Published    1977 
  Keywords    Sulfate Reduction, Energy Charge, Chloroplasts, Adenine Nucleotides, ATP-Sulfurylase 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0792.pdf 
 Identifier    ZNC-1977-32c-0792 
 Volume    32 
2Author    Divya Mishra, Ahlert SchmidtRequires cookie*
 Title    Regulation and Partly Purification of the ATP-Sulfurylase from the Cyanobacterium Synechococcus 6301  
 Abstract    ATP-sulfurylase from the cyanobacterium Synechococcus 6301 was regulated in vivo during growth in batch culture. The activity was highest at the third day after inoculation, declining afterwards to a level found in resting cells. During growth with air supplemented with 2% CO, this activity increased 3-fold compared to controls grown with normal air as C 0 2 source. Addition o f either nitrite or urea enhanced ATP-sulfurylase activity about 2-fold, whereas cys­ teine and especially methionine decreased ATP-sulfurylase activity to 5% o f controls without treatment. The ATP-sulfurylase was purified by conventional techniques using D EAE-cellulose chro­ matography and further separation on blue sepharose achieving a 250-fold increase in the spe­ cific activity. An apparent o f 5 for APS and o f 40 |iM for pyrophosphate was deter­ mined with the purified enzyme fraction. 
  Reference    Z. Naturforsch. 47c, 95 (1992); received September 26 1991 
  Published    1992 
  Keywords    ATP-Sulfurylase, Cyanobacterium, Synechococcus, Sulfate A ctivation, Regulation 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0095.pdf 
 Identifier    ZNC-1992-47c-0095 
 Volume    47