1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

This is an abbreviated version, for detailed information about sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming), go to the full flat file.

Reaction

L-erythro-7,8-dihydrobiopterin
+
NADP+
=
sepiapterin
+
NADPH
+
H+

Synonyms

AKR1B1, reductase, sepiapterin, sepiapterin reductase, SPR, SR

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.153 sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

Crystallization

Crystallization on EC 1.1.1.153 - sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified native and selenomethionine-labeled enzyme alone and in complex with NADP+ and sepiapterin, hanging drop vapour diffusion method, 18°C, 0.004 ml protein solution, with or without 10 mM NADP+ and sepiapterin, is mixed with 0.001 ml of a mixture of 0.004 ml or reservoir solution containing 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, and 34% PEG 400, and 0.001 ml additive solution 1 M guanidinium hydrochloride, X-ray diffraction structure determination and analysis at 2.1 A and 1.7 A resolution, respectively
-
purified native and selenomethionine-labeled enzyme, hanging drop vapour diffusion microbatch method, 18°C, 0.004 ml protein solution containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, is mixed with 0.001 ml of a mixture of 0.004 ml or reservoir solution containing 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, and 34% PEG 400, and 0.001 ml additive solution 1 M guanidinium hydrochloride, 2 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
vapour diffusion technique