Interaction of muscle glycogen phosphorylase b reconstituted from apoenzyme and analogs of pyridoxal-5'-phosphate with specific ligands.
Phosphorylase b from rabbit skeletal muscles was reconstituted with analogs of PLP containing residues -CH(2)-CH(2)-COOH, trans-CH=CH-COOH or -C=-COOH at position 5. Replacing native coenzyme in the phosphorylase molecule with any PLP analog tested leads to the decrease in the enzyme affinity for the allosteric inhibitor, FMN. Phosphorylase b reconstituted with analogs of PLP shows the greater ability for association in tetramers in the presence of 1 mM AMP than native enzyme.
Chebotareva
N A
NA
Scientific Manufacturing Association "Vitaminy", Ministry of Health and Medicine Industry, Moscow, Russia.
Sugrobova
N P
NP
Bulanova
L N
LN
Poznanskaya
A A
AA
Kurganov
B I
BI
Gunar
V I
VI
D000818:Animals; D008024:Ligands; D018482:Muscle, Skeletal / Q000201:enzymology*; D010763:Phosphorylase b / Q000737:chemistry / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism*; D011817:Rabbits
D008024:Ligands; D011732:Pyridoxal Phosphate; D010763:Phosphorylase b