1.1.1.325: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)

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For detailed information about sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming), go to the full flat file.

Reaction

Synonyms

MDSPR, sepiapterin reductase, SPR

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.325 sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)

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Results	in table
93	AA Sequence
3	Cloned(Commentary)
3	Cofactor
1	Crystallization (Commentary)
1	Expression
3	General Information
1	General Stability
2	Inhibitors
1	Ki Value [mM]
5	KM Value [mM]
1	Localization
4	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
3	Organism
2	Pathway
3	pH Optimum
1	pH Range
3	Purification (Commentary)
2	Reaction
3	Reference
12	Source Tissue
7	Substrates and Products (Substrate)
3	Subunits
5	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.325 - sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)

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purified recombinant His-tagged wild-type and selenomethionine-substituted enzymes, hanging drop vapour diffusion method at 18°C, mixing of 0.004 ml of protein solution containing 10 mg/ml in 20 mM Tris-HCl, pH 8.0, by ultrafiltration, with 0.001 ml of reservoir solution containing 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, 34% PEG 400, and 0.2 M guanidine hydrochloride, screening and method optimization, crystals of the wild-type enzyme are soaked in reservoir solution containing 1 mM NADP+ and 1 mM sepiapterin or containing 1 mM NADP+ and 1 mM N-acetylserotonin, respectively, X-ray diffraction structure determination and analysis at 2.1 A resolution

Chlorobaculum tepidum

667067