Albumin and alkaline phosphatase as factors involved in the regulation of tyrosine phenol-lyase activity.
Holotyrosine phenol-lyase (EC 4.1.99.2), a pyridoxal-5'-phosphate (PLP)- requiring enzyme, was shown to rapidly dissociate when injected into BDF1 mice. The holoenzyme dissociated when incubated in plasma but not 0.01 M potassium phosphate (pH 7.4) buffer at 37 degrees C. A nonspecific alkaline phosphatase from calf intestine was found to inactivate the holoenzyme at pH 7.4 and 37 degrees C. This inactivation was inhibited in the presence of 0.5 M potassium phosphate buffer. Two other PLP-requiring enzymes, aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2) were inactivated by alkaline phosphatase in a similar manner. Incubation of holotyrosine phenol-lyase in the presence of bovine serum albumin also resulted in a reduction of holoenzyme activity but partially protected the enzyme from inactivation by alkaline phosphatase. A nuclear fraction having PLP-hydrolyzing activity also inactivated holotyrosine phenol-lyase. A regulatory function for alkaline phosphatase in the metabolism of PLP-requiring enzymes is suggested by these data.
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D005260:Female; D006207:Half-Life; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure; D008190:Lyases / Q000378:metabolism*; D051379:Mice; D011732:Pyridoxal Phosphate / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism*; D013997:Time Factors; D014447:Tyrosine Phenol-Lyase / Q000097:blood / Q000378:metabolism*
D012709:Serum Albumin; D011732:Pyridoxal Phosphate; D000469:Alkaline Phosphatase; D008190:Lyases; D014447:Tyrosine Phenol-Lyase