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Kawh t?l al.: Intermediates of sepiapterin reductase reaction Pteridines Vol. 4, 1993, pp. 90-92 Short Communication Setsuko Katoh §, Terumi Sueoka , Masahiro Masada t and Harumi Hikita t li Department of Biochemistry, Meikai University School of Dentistry, Sakado, Saitama 350-02, Japan t Laboratory of Biochemistry, Faculty of Horticulture, Chiba Univ., Matsudo, Chiba 648, Japan tLaboratory of Physics, Meikai University, Urayasu, Chiba 279, Japan (Received February 1, 1993) Introduction pyruvoy\ PH4 Sepiapterin reductase [EC 1.1.1.153J is now known to be involved in the last pathway of the biosynthesis of tetrahydrobiopterin (BH4). The enzyme catalyzes 6-pyruvoyl tetrahydropterin (PPH 4), the key metabolic substance in the pathway from GTP. This enzyme was originally defined as the enzyme that reduces sepiapterin specifically. The specificity of the enzyme for sepiapterin has been beleived for the past 20 years. But in 1984 (1), we found that this enzyme along with NADPH could also reduce various carbonyl substances including diketo compounds other than sepiapterin. This broad specificity of the enzyme for carbonyl compounds indicated that sepiapterin reductase belongs to the group of so-called aldo-keto reductases, especially carbonyl reductase (2). After this finding, many workers confirmed that both of the vicinal carbonyls of PPH4 can
Pteridines – de Gruyter
Published: May 1, 1993
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