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Pteridine-metabolizing enzymes of Macaca fascicularis
Abstract:
1. The crab-eating monkey (Macaca fascicularis) has been studied for enzymes which react in the biosynthesis of pteridine cofactor of phenylalanine hydroxylase: 2. Rather high activity of sepiapterin reductase (EC 1.1.1.153)(0.130 mumol) and measurable activity of dihydrofolate reductase (EC 1.5.1.3)(0.039 mumol), (in amount of substrate reduced/hr/mg protein at 37 degrees C) were found in the crude extract from the liver. 3. Sepiapterin reductase was observed, in blood, only in the erythrocytes while dihydrofolate reductase was observed both in erythrocytes and leucocytes. 4. Activity of pteridine cofactor of phenylalanine hydroxylase was detected in the extract of the liver. 5. Sepiapterin reductase was partially purified from the liver, and was studied in the mol. wt, coenzyme-requirement, pH optimum, KmS and inhibitors.
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