Go toArchive
Browse byFacets
Bookbag ( 0 )
'Fructosebisphosphatase' in keywords Facet   Publication Year 1996  [X]
Results  1 Item
Sorted by   
Publication Year
1Author    N. G. RotjohannRequires cookie*
 Title    Regulation of Fructose 1,6-Bisphosphatase Activity of Chlorella by Mole Mass Change  
 Abstract    Fast protein liquid chromatography on Superose 6 of partially purified FBPase II from Chlorella reveals a 1350 kDa-form at pH 6.0 and a 67 kDa-form at pH 8.5. Treatment o f the large enzyme form with 5mM concentrations of Mg2+, F1,6P2, DTT or ATP leads to dissoci­ ation into smaller ones of 2 1 5 -4 7 0 kDa. Aggregation/dissoziation is a reversible process, as has been shown for the effect of F1,6P2 and of pH, by rechromatography. The change in m ole mass results in alterations of the activitiy and of the kinetic properties of the enzyme forms, obtained. Dissociation results in a 4 -6 fold increase in activity, as can be shown for F l,6 P2-treated samples. Halfsaturation constants, as well as the degree o f cooperativity of the 67-and the 1350-kDa form, are different for substrate affinity, activation by Mg2+ and DTT, and for inhibition by ATP. Both enzyme forms hydrolyse fructose 1,6 bisphosphate and seduheptulose 1,7 bis­ phosphate better than other phosphorylated compounds. The ratio o f F1,6P2-to SDP-cleav-age is 100:58 for the small enzym e form and 100: 84 for the large one. Activation of FBPase II in the light and inactivation in the dark is discussed on the basis of different oligomeric forms of the enzyme, generated by changes in the concentration of intermediates and effectors in the chloroplast stroma, leading to dissociation or aggregation. The conclusion is drawn that oligomerization of key enzymes, resulting in enzyme forms with different activities and different kinetic properties, might provide an effective mechanism for enzyme regulation in vivo. 
  Reference    Z. Naturforsch. 51c, 639 (1996); received September 14 1995/March 7 1996 
  Published    1996 
  Keywords    Chlorella, Fructosebisphosphatase, Oligomerization Activation Kinetic Properties 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0639.pdf 
 Identifier    ZNC-1996-51c-0639 
 Volume    51