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.
Word Map on EC 1.1.1.153
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1.1.1.153
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tetrahydrobiopterin
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bh4
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aldo-keto
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cyclohydrolase
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aldose
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neurotransmitter
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pterins
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dopa-responsive
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tetrahydropterins
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6-pyruvoyl-tetrahydropterin
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n-acetylserotonin
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dystonia
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dihydropteridine
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dihydroneopterin
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6-pyruvoyl
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pteridine
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neopterin
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gtpch
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ptges
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gtp-cyclohydrolase
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5-hydroxytryptophan
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akr1b3
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6r-5,6,7,8-tetrahydrobiopterin
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epalrestat
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hyperphenylalaninaemia
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segawa
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2,4-diamino-6-hydroxypyrimidine
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medicine
- 1.1.1.153
- tetrahydrobiopterin
- bh4
-
aldo-keto
-
cyclohydrolase
- aldose
-
neurotransmitter
- pterins
-
dopa-responsive
- tetrahydropterins
- 6-pyruvoyl-tetrahydropterin
- n-acetylserotonin
- dystonia
- dihydropteridine
- dihydroneopterin
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6-pyruvoyl
- pteridine
- neopterin
- gtpch
- ptges
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gtp-cyclohydrolase
- 5-hydroxytryptophan
- akr1b3
- 6r-5,6,7,8-tetrahydrobiopterin
- epalrestat
- hyperphenylalaninaemia
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segawa
- 2,4-diamino-6-hydroxypyrimidine
- medicine
Reaction
Synonyms
AKR1B1, MDSPI16 protein, MDSPR, reductase, sepiapterin, sepiapterin reductase, SPR, SR
ECTree
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General Information
General Information on EC 1.1.1.153 - sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
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malfunction
metabolism
physiological function
additional information
RNAi-mediated knockdown of SPR expression significantly reduces native ornithine decarboxylase enzyme activity and impedes neuroblastoma cell proliferation
malfunction
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tetrahydrobiopterin deficiencies are implicated in neuronal disorders. Drosophile melanogastersloss-of-function enzyme mutants are resonsibel for hyposensitivityy to oxidative stress, enzyme activity and tetrahydrobiopterin levels in the mutants are significantly reduced compared to wild-type, while levels of phosphorylated Akt and total Akt protein are increased in the enzyme mutants
malfunction
the knockdown of SPR leads to a significant and consistent decrease in cellular proliferation of neuroblastoma cells
malfunction
enzyme inhibition reduces pain hypersensitivity in a mouse model of joint inflammation
sepiapterin reductase (SPR) catalyzes the final steps of tetrahydrobiopterin (BH4) biosynthesis
metabolism
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sepiapterin reductase is a key enzyme in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for the synthesis of important biogenic amines, including catecholamines and serotonin
metabolism
the enzyme plays an important role in the biosynthesis of tetrahydrobiopterin
high SPR expression is significantly correlated to unfavorable neuroblastoma characteristics like high age at diagnosis, MYCN oncogene amplification, and high INSS disease stage. Sulfasalazine inhibits the growth of neuroblatoma cells in vitro, presumably due to the inhibition of sepiapterin reductase
physiological function
in PC12 cells, which generate catecholamine and monoamine neurotransmitters via BH4-dependent amino acid hydroxylases, sulfa drugs inhibit both dihydrobiopterin/tetrahydrobiopterin biosynthesis and redox cycling mediated by sepiapterin reductase. Inhibition of dihydrobiopterin/tetrahydrobiopterin biosynthesis results in decreased production of dopamine and dopamine metabolites, 3,4-dihydroxyphenylacetic acid and homovanillic acid, and 5-hydroxytryptamine
physiological function
native ornithine decarboxylase and sepiapterin reductase physically interact. The resulting heterocomplex is a compact structure, featuring two energetically and structurally equivalent binding modes both in monomer and dimer conformations. siRNA-mediated knock-down of sepiapterin reductase expression significantly reduces endogenous ornithine decarboxylase enzyme activity in neuroblastoma cells
physiological function
sepiapterin reductase (SPR) catalyzes the final steps of tetrahydrobiopterin (BH4) biosynthesis. BH4 is an essential cofactor for aromatic acid hydroxylases and nitric oxide synthase. BH4 deficiency causes endothelial dysfunction, such as hypertension, atherosclerosis, diabetes, etc.
physiological function
sepiapterin reductase (SPR) catalyzes the last step in the biosynthesis of tetrahydrobiopterin (BH4) by converting 6-pyruvoyl tetrahydropterin to tetrahydrobiopterin. BH4 is an essential cofactor of nitric oxide synthase (NOS), which converts arginine to nitric oxide (NO) and citrulline in the urea cycle. Native ornithine decarboxylase, ODC, EC 4.1.1.17, and sepiapterin reductase physically interact, SPR is a regulator of ODC activity. SPR is implicated in neurological diseases and in cancer. SPR contributes to neuroblastoma cell proliferation and regulates ODC enzyme activity in neuroblastoma cells, ODC-SPR interaction controls polyamine-driven cellular proliferation
physiological function
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sepiapterin reductase plays an important role in the Akt pathway
physiological function
using NADPH as a source of reducing equivalents, sepiapterin reductase (SPR) catalyzes the reduction of sepiapterin to dihydrobiopterin (BH2), a precursor for tetrahydrobiopterin (BH4). Reduction of sepiapterin generates 7,8-dihydrobiopterin, which is converted to (6R)-5,6,7,8-tetrahydrobiopterin by additional cellular reductases
physiological function
using NADPH as a source of reducing equivalents, sepiapterin reductase (SPR) catalyzes the reduction of sepiapterin to dihydrobiopterin (BH2), a precursor for tetrahydrobiopterin (BH4). Reduction of sepiapterin generates 7,8-dihydrobiopterin, which is converted to (6R)-5,6,7,8-tetrahydrobiopterin by additional cellular reductases
computational docking of inhibitor sulfasalazine into sepiapterin reductase using crystal structure of human SPR in complex with NADP+ in a hexameric assembly, PDB ID 1Z6Z
additional information
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computational docking of inhibitor sulfasalazine into sepiapterin reductase using crystal structure of human SPR in complex with NADP+ in a hexameric assembly, PDB ID 1Z6Z
additional information
enzyme three-dimensional structure molecular modeling and docking using crystal structures of SPR, PDB IDs 1SEP, 1NAS, 4HWK, 4J7U, and 4J7X, and the structure of menadione, PDB ID 2QR2, overview
additional information
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enzyme three-dimensional structure molecular modeling and docking using crystal structures of SPR, PDB IDs 1SEP, 1NAS, 4HWK, 4J7U, and 4J7X, and the structure of menadione, PDB ID 2QR2, overview