Metabolic regulation of glycolysis in sea bass (Dicentrarchus labrax L.) muscle. I. Kinetic study and characteristic modulators of pyruvate kinase.
White muscle pyruvate kinase from sea bass presents positive cooperativity with respect to PEP substrate. The enzyme is regulated by F-1.6-P2 and L-Phenylalanine. The activator effect of F-1.6-P2 in experiments carried out for the substrate PEP with crude extract seems to indicate that the enzyme is activated in vivo by this compound. The enzyme was not inhibited by either alanine or ATP but was inhibited by L-phenylalanine. Therefore this enzyme presents kinetic and regulatory properties similar to those of the mammalian isozyme M2.
Fideu
M D
MD
Departamento de Bioquímica, Facultad de Veterinaria, Universidad Complutense, Madrid.
Maroto
M L
ML
Serradilla
M C
MC
Pérez
M L
ML
Herranz
M J
MJ
Ruiz-Amil
M
M
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000409:Alanine / Q000378:metabolism; D000818:Animals; D001492:Bass; D004789:Enzyme Activation; D005635:Fructosediphosphates / Q000378:metabolism*; D006019:Glycolysis; D006598:Hexosediphosphates / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D010649:Phenylalanine / Q000378:metabolism*; D010728:Phosphoenolpyruvate / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism*
D005635:Fructosediphosphates; D006598:Hexosediphosphates; D010649:Phenylalanine; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D011770:Pyruvate Kinase; C029063:fructose-1,6-diphosphate; D000409:Alanine