Pyridoxal 5'-phosphate as a catalytic and conformational cofactor of muscle glycogen phosphorylase B.
This review summarizes data on structure of muscle glycogen phosphorylase b and the role of the cofactor pyridoxal 5'-phosphate in catalysis and stabilizing the native conformation of the enzyme. Specific attention is paid to the stabilizing role of pyridoxal 5'-phosphate upon denaturation of phosphorylase b. Stability of holoenzyme, apoenzyme, and enzyme reduced by sodium borohydride is compared.
Livanova
N B
NB
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071 Russia. livanova@inbi.ras.ru
Chebotareva
N A
NA
Eronina
T B
TB
Kurganov
B I
BI
D000818:Animals; D002384:Catalysis; D004795:Enzyme Stability; D024982:Glycogen Phosphorylase, Muscle Form / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D018482:Muscle, Skeletal / Q000201:enzymology*; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000737:chemistry / Q000378:metabolism*
D011732:Pyridoxal Phosphate; D024982:Glycogen Phosphorylase, Muscle Form