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

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The expected taxonomic range for this enzyme is: Chlorobaculum tepidum

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EC NUMBER
COMMENTARY hide
1.1.1.325
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RECOMMENDED NAME
GeneOntology No.
sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
show the reaction diagram
(1)
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L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrahydrobiopterin biosynthesis III
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SYSTEMATIC NAME
IUBMB Comments
L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase
This enzyme, isolated from the bacterium Chlorobium tepidum, catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. cf. EC 1.1.1.153, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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alignment of amino acid sequences near the N-termini of sepiapterin reductases from various sources, overview
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-pyruvoyl-5,6,7,8-tetrahydropterin + 3 NADPH + 3 H+
L-threo-7,8-dihydrobiopterin + 3 NADP+
show the reaction diagram
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?
6-pyruvoyl-5,6,7,8-tetrahydropterin + NADPH + H+
L-threo-7,8-dihydrobiopterin + NADP+
show the reaction diagram
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?
diacetyl + NADPH + H+
? + NADP+
show the reaction diagram
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?
L-threo-7,8-dihydrobiopterin + NADP+
sepiapterin + NADPH + H+
show the reaction diagram
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r
additional information
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the enzyme also shows activity with D-threo-dihydrobiopterin, L-threo-dihydroneopterin, and dihydrotepidopterin, and low activity with L-erythro-dihydrobiopterin
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-pyruvoyl-5,6,7,8-tetrahydropterin + 3 NADPH + 3 H+
L-threo-7,8-dihydrobiopterin + 3 NADP+
show the reaction diagram
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?
6-pyruvoyl-5,6,7,8-tetrahydropterin + NADPH + H+
L-threo-7,8-dihydrobiopterin + NADP+
show the reaction diagram
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetyldopamine
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additional information
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N-acetylserotonin and melatonin are no inhibitors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
diacetyl
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pH 8.8, 45°C
0.0062
NADPH
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pH 8.8, 45°C
0.021
sepiapterin
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pH 8.8, 45°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
NADPH
Chlorobaculum tepidum
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pH 8.8, 45°C
5
sepiapterin
Chlorobaculum tepidum
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pH 8.8, 45°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
N-acetyldopamine
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pH 8.8, 45°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 26000, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability of the purified enzyme disappears in sodium citrate buffer and potassium phosphate buffer for 24 h at 4°C, it increases continuously in Tris-HCl buffer and in glycine/NaOH buffer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 533fold from cytosol by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration followed by affinity chromatography, another different step of anion exchange chromatography, and ultrafiltration
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recombinant His-tagged wild-type and selenomethionine-substituted enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, anion exchange chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and selenomethionine-substituted enzymes in Escherichia coli strain BL21(DE3)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.325)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)