[Aspartate kinase activity of Cyanobacteria Anabaena variabilis].
Aspartate-kinase (ASK) activity of filamentous cyanobacteria A. variabilis and its dependence on physico-chemical factors and substrate concentration in the reaction mixture have been studied. Three isoenzymes ASK-1, ASK-2 and ASK-3 which differ in the values of pH-optima, molecular weight, isoelectric points and effector of retro-inhibition have been isolated by ion-exchange chromatography. High level of inhibition of summary ASK of the cell-free extract can be reached only in a case of simultaneous addition of all amino acids, the final products of this biosynthetic pathway into the incubation mixture.
Lysenko
T G
TG
Koltukova
N V
NV
Kadyrova
G Kh
GKh
Shainskaia
O A
OA
D001222:Aspartate Kinase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D000458:Cyanobacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight
D007527:Isoenzymes; D001222:Aspartate Kinase
Aspartatkinaznaia aktivnost' tsianobakterii Anabaena variabilis.