Results 141 to 150 of about 107,475 (169)

Sepiapterin Reductase and ALR2 (“Aldose Reductase”) from Bovine Brain

1993
Sepiapterin reductase (EC 1.1.1.153) catalyses the NADPH-dependent reduction of L-sepiapterin to 7,8-dihydrobiopterin as shown in Fig.1. It was first described in silkworms where it was shown to be a separate enzyme from Dihydrofolate reductase (Matsubara et al., 1963).
T G, Dowling, J F, O'Rourke, K F, Tipton
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Sepiapterin reductase in blood of various animals and of leukemic rats

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract The level of sepiapterin reductase (EC 1.1.1.153) activity in blood of various animals was examined with special reference to dihydrofolate reductase activity. Both enzyme activities in liver were determined for comparison. In all animal species tested, the activity of sepiapterin reductase was only found in erythrocytes though ...
S, Katoh, Y, Arai, T, Taketani, S, Yamada   +3 more
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Characterization of sepiapterin reductase activity from Drosophila melanogaster

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1996
A kinetic study of Drosophila melanogaster sepiapterin reductase has been done. The apparent Km for sepiapterin has been estimated as 153 microM. N-acetyldopamine, N-acetylserotonin, and N-methoxyacetylserotonin have shown to be noncompetitive inhibitors for the Drosophila sepiapterin reductase. The Ki obtained were 40 microM, 127 microM and 87 microM,
P, Ruiz-Vázquez, F J, Silva, J, Ferré
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Direct inhibition of brain sepiapterin reductase by a catecholamine and an indoleamine

Biochemical and Biophysical Research Communications, 1982
Summary Rat brain sepiapterin reductase, which is involved in the biosynthesis of tetrahydrobiopterin, was directly inhibited by a catecholamine and an indoleamine which require tetrahydrobiopterin as a cofactor in the biosyntheses of themselves.
S, Katoh, T, Sueoka, S, Yamada
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On the presence of sepiapterin reductase different from folate and dihydrofolate reductase in chicken liver

Experientia, 1964
Nous avons demontre dans le foie de poussin l'existence d'un ferment qui reduit specifiquement la sepiapterine. Il est capable de separer le ferment de reductase d'acide folique et d'acide dihydrofolique apres precipitation fractionnaire de sulfate d'ammonium.
M, Matsubara, M, Akino
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Purification and Properties of Human Sepiapterin Reductase from Placenta

1993
Recently H4biopterin was found to be synthesized in cells which do not use it as a hydroxylation cofactor. This is the case during cytokine-directed proliferation and differentiation of cells which participate in hematopoiesis or immune response ...
J, Maier, I, Ziegler
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Studies on sepiapterin reductase: Further characterization of the reaction product

Archives of Biochemistry and Biophysics, 1968
Abstract Sepiapterin reductase from rat liver catalyzes reduction of sepiapterin in the presence of NADPH. The reaction product was isolated from the reaction mixture via Sephadex column chromatography and its properties were compared with those of synthetic dihydrobiopterin.
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Sepiapterin reductase

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
M, Matsubara, S, Katoh, M, Akino, S, Kaufman   +3 more
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Isomerization of 6-lactoyl tetrahydropterin by sepiapterin reductase.

Journal of biochemistry, 1987
Isomerization of 6-1'-oxo-2'-hydroxypropyl tetrahydropterin (6-lactoyl tetrahydropterin) to 6-1'-hydroxy-2'-oxopropyl tetrahydropterin has been attributed to sepiapterin reductase. The activity is N-acetylserotonin-insensitive and has a well defined pH optimum of 8.6.
S, Katoh, T, Sueoka
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Sepiapterin reductase

1995
Dietmar Schomburg, Dörte Stephan
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