Abstract
It is shown that 2-chloroacetaldehyde, iodoacetamide and bromopyruvate irreversibly inactive the serine transhydroxymethylase ( l-serine:tetrahydrofolate 5,10-hydroxymethyltransferase, EC 2.1.2.1) and threonine aldolase ( l-threonine acetaldehyde-lyase, EC 4.1.2.5) activities in a coordinated fashion. Glycine, l-serine and dl-allothreonine partially protect both the activities against inactivation. These results confirm the conclusion of Schirch and Gross 8 that the serine transhydroxymethylase and threonine aldolase activities from the rabbit liver may be the property of the same or very similar enzymes.
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