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4 alpha-Hydroxy-tetrahydropterin dehydratase
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4-alpha-hydroxy-tetrahydropterin dehydratase
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4-alpha-hydroxytetrahydrobiopterin dehydratase
UniProt
4a-Carbinolamine dehydratase
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4a-Hydroxytetrahydrobiopterin dehydratase
4a-Hydroxytetrahydropterin dehydratase
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carbinolamine-4a-dehydratase
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DcoH2
dimerization cofactor of HNF1alpha
Dehydratase, 4a-carbinolamine
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Dimerization cofactor of hepatocyte nuclear factor 1-alpha
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Dimerization cofactor of HNF1
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Dimerization factor of HNF1/pterin-4alpha-carbinolamine dehydratase
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GenBank AE000671-derived protein GI 2982796
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Phenylalanine hydroxylase-stimulating protein
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Phenylalanine hydroxylase-stimulating protein/pterin-4alpha-carbinolamine dehydratase
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pterin 4a-carbinolamine dehydratase
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Pterin carbinolamine dehydratase
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Pterin-4 alpha-carbinolamine dehydratase
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Pterin-4-alpha-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
Pterin-4a-carbinolamine dehydratase (Aquifex aeolicus gene phhB)
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Pterin-4a-carbinolamine dehydratase/dimerization cofactor of HNF1
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Pterin-4alpha-carbinolamine dehydratase
Pterin-4alpha-carbinolamine dehydratase (PCD)/dimerization cofactor for the transcription factor HBF-1alpha
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4a-Hydroxytetrahydrobiopterin dehydratase
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4a-Hydroxytetrahydrobiopterin dehydratase
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DCoHalpha
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PCD
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PCD/DCoH
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4a-carbinolamine dehydratase
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Pterin-4alpha-carbinolamine dehydratase
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Pterin-4alpha-carbinolamine dehydratase
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Pterin-4alpha-carbinolamine dehydratase
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additional information
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the enzyme has identical amino acid sequence to DCoH, the dimerization cofactor of the transcription regulator, HNF-1alpha
additional information
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the enzyme is identical with the dimerization cofactor DCoH, a cofactor for the hepatocyte nuclear factor 1alpha, HNF1alpha, which is essential for expression of phenylalanine hydroxylase PAH EC 1.14.16.1
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(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
4a(R)-hydroxy-6(S)-methyltetrahydropterin
quinoid 6(S)-methyldihydropterin
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4a(R)-hydroxy-6(S)-propyltetrahydropterin
quinoid 6(S)-propyldihydropterin
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4a(S)-hydroxy-6(R)-methyltetrahydropterin
quinoid 6(R)-methyldihydropterin
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4a-Hydroxy-6(R)-dihydroxypropyltetrahydropterin
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4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
4a-Hydroxy-6(S)-propyltetrahydropterin
Quinoid 6(S)-propyldihydropterin
4a-hydroxy-tetrahydrobiopterin
7,8-dihydrobiopterin + H2O
4a-hydroxy-tetrahydropterin
7,8-dihydropterin + H2O
4a-hydroxytetrahydrobiopterin
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4alpha-hydroxy-6(S)-methyltetrahydropterin
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6(S)-methyl-4a-hydroxy-tetrahydropterin
6(S)-methyl-7,8-dihydropterin + H2O
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6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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6,6-dimethyl-4a-hydroxy-tetrahydropterin
6,6-dimethyl-7,8-dihydropterin + H2O
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pterin-4alpha-carbinolamine
quininoid dihydropterin + H2O
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additional information
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(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
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(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
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(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O
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4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
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4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
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4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
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4a-Hydroxy-6(S)-propyltetrahydropterin
Quinoid 6(S)-propyldihydropterin
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4a-Hydroxy-6(S)-propyltetrahydropterin
Quinoid 6(S)-propyldihydropterin
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4a-hydroxy-tetrahydrobiopterin
7,8-dihydrobiopterin + H2O
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4a-hydroxy-tetrahydrobiopterin
7,8-dihydrobiopterin + H2O
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4a-hydroxy-tetrahydropterin
7,8-dihydropterin + H2O
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4a-hydroxy-tetrahydropterin
7,8-dihydropterin + H2O
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6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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additional information
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a defect in 4a-hydroxytetrahydrobiopterin dehydratase provoces the conversion of the 6-substituted pterins to their 7-substituted isomers
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additional information
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the mutant enzyme form C82R and the 18-amino acid-truncated mutant Glu87-termination occur naturally associated with hyperphenyalaninemia
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additional information
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the codevelopment of 4a-hydroxytetrahydropterin dehydratase with dihydropteridine reductase strongly supports a physiologically significant role for the dehydratase in tetrahydrobiopterin regeneration
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additional information
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the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
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additional information
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the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
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additional information
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dehydratase/DCoHalpha, has the kinetic properties necessary for regenerating tetrahydrobiopterin cofactor for phenylalanine hydroxylase. Properties of dehydratase/DCoHalpha are consistent with the hypothesis that the activity of this isozyme could account for the relatively mild symptoms reported for patients with a defect in dehydratase/DCoH
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additional information
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DCoHalpha is coactivator of HNF1alpha-depndent transcription
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additional information
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both PhhB and phenylalanine hydroxylase (PhhA) are induced coordinately in the presence of either L-tyrosine or L-phenylalanine, but PhhB exhibits a significant basal level of activity that is lacking for PhhA. PhhA and PhhB form a protein-protein complex
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additional information
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additional information
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the enzyme may not play an important role in the regulation of the synthesis of those neurotransmitters which are derived from the hydroxylated aromatic amino acids
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additional information
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the enzyme is essential in vivo to prevent rearrangement of 4a-hydroxy-6(R)-tetrahydrobiopterin and to maintain the supply of tetrahydrobiopterin cofactor for hydroxylases under conditions where the nonenzymatic rate would be inadequate
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additional information
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the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
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additional information
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the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
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additional information
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enzyme plays a role in the regulation of expression of phenylalanine hydroxylase via transcription factor HNF1alpha
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4a-hydroxytetrahydrobiopterin dehydratase deficiency
7-substituted pterins in humans with suspected pterin-4a-carbinolamine dehydratase deficiency. Mechanism of formation via non-enzymatic transformation from 6-substituted pterins.
4a-hydroxytetrahydrobiopterin dehydratase deficiency
International database of tetrahydrobiopterin deficiencies.
4a-hydroxytetrahydrobiopterin dehydratase deficiency
Suspected pterin-4a-carbinolamine dehydratase deficiency: hyperphenylalaninaemia due to inhibition of phenylalanine hydroxylase by tetrahydro-7-biopterin.
4a-hydroxytetrahydrobiopterin dehydratase deficiency
[Screening of tetrahydrobiopterin deficiency among hyperphenylalaninemic patients]
6,7-dihydropteridine reductase deficiency
International database of tetrahydrobiopterin deficiencies.
6-pyruvoyltetrahydropterin synthase deficiency
International database of tetrahydrobiopterin deficiencies.
Colonic Neoplasms
Dimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesions.
Colonic Neoplasms
Overexpression of pterin-4a-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 in human colon cancer.
Colorectal Neoplasms
Overexpression of pterin-4a-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 in human colon cancer.
Dehydration
Catalytic characterization of 4a-hydroxytetrahydropterin dehydratase.
Dehydration
Distribution of 4a-hydroxytetrahydropterin dehydratase in rat tissues. Comparison with the aromatic amino acid hydroxylases.
Dehydration
Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase.
gtp cyclohydrolase i deficiency
International database of tetrahydrobiopterin deficiencies.
Melanoma
Dimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesions.
Neoplasms
Dimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesions.
Neoplasms
Overexpression of pterin-4a-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 in human colon cancer.
Phenylketonurias
Four Years of Diagnostic Challenges with Tetrahydrobiopterin Deficiencies in Iranian Patients.
Phenylketonurias
Homomeric and heteromeric interactions between wild-type and mutant phenylalanine hydroxylase subunits: evaluation of two-hybrid approaches for functional analysis of mutations causing hyperphenylalaninemia.
Phenylketonurias
International database of tetrahydrobiopterin deficiencies.
Phenylketonurias
Suspected pterin-4a-carbinolamine dehydratase deficiency: hyperphenylalaninaemia due to inhibition of phenylalanine hydroxylase by tetrahydro-7-biopterin.
Phenylketonurias
Tetrahydrobiopterin and inherited hyperphenylalaninemias.
Vitiligo
Crystallization and preliminary crystallographic studies of recombinant dimerization cofactor of transcription factor HNF1/pterin-4 alpha-carbinolamine dehydratase from liver.
Vitiligo
Defective tetrahydrobiopterin and catecholamine biosynthesis in the depigmentation disorder vitiligo.
Vitiligo
Dimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesions.
Vitiligo
Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1.
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0.004 - 0.0053
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
0.006 - 390
4a(R)-hydroxy-6(S)-methyltetrahydropterin
0.0015
4a(R)-hydroxy-6(S)-propyltetrahydropterin
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pH 8.4 or pH 7.4
0.0015 - 0.03
4a(S)-hydroxy-6(R)-methyltetrahydropterin
0.0025 - 0.003
4a-Hydroxy-6(S)-methyltetrahydropterin
0.0013
4a-Hydroxy-6(S)-propyltetrahydropterin
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fetal and adult enzyme
0.0047 - 0.0052
4a-hydroxytetrahydrobiopterin
0.007 - 2.2
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
additional information
additional information
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0.004
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
wild-type
0.0044
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
Q45R/K98Q
0.0052
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
N61D
0.0053
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
N61D/Q45R/K98Q
0.006
4a(R)-hydroxy-6(S)-methyltetrahydropterin
wild type enzyme
330
4a(R)-hydroxy-6(S)-methyltetrahydropterin
mutant enzyme H62A
390
4a(R)-hydroxy-6(S)-methyltetrahydropterin
mutant enzyme H61A
0.0015
4a(S)-hydroxy-6(R)-methyltetrahydropterin
wild type enzyme
0.0025
4a(S)-hydroxy-6(R)-methyltetrahydropterin
mutant enzyme H79A
0.03
4a(S)-hydroxy-6(R)-methyltetrahydropterin
mutant enzyme H62A
0.0025
4a-Hydroxy-6(S)-methyltetrahydropterin
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pH 8.4 or pH 7.4
0.003
4a-Hydroxy-6(S)-methyltetrahydropterin
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10°C, pH 7.4
0.0047
4a-hydroxytetrahydrobiopterin
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mutant enzyme C82R
0.0052
4a-hydroxytetrahydrobiopterin
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wild type enzyme
0.007
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme Tyr69Thr
0.008
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme Y69F
0.01
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme H79A
0.012
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme His79Ser
0.017
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme Cys81Arg
0.018
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme D60A
0.02
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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0.02
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme Arg87Ala
0.02
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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wild type enzyme and mutant enzyme G72D
0.025
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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wild type enzyme
0.025
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme E69A
0.04
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme Cys81Ser
0.06
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme H91A
0.075
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme H62A
2.2
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
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mutant enzyme H61A
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malfunction
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PCD deficiency causes in newborns a mild form of hyperphenylalaninaemia with persistent high urinary levels of primapterin. Affected patients appear completely normal, but have elevated phenylalanine levels at birth, which normalize after few months of life and remain normal or just above the normal range of phenylalanine with an unrestricted diet
malfunction
a Mu transposon insertion in the Zea mays (maize) gene encoding a chloroplast dimerization co-factor of hepatocyte nuclear factor 1 (DCoH)/pterin-4a-carbinolamine dehydratases (PCD)-like protein is the causative mutation in a seedling-lethal, Rubisco-deficient mutant named Rubisco accumulation factor 2 (raf2-1). In raf2 mutants newly synthesized Rubisco large subunit accumulates in a high-molecular weight complex, the formation of which requires a specific chaperonin 60-kDa isoform. raf2 Mutant phenotype, overview
malfunction
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in mutant phenotype lemon, the expression of BmDhpr is activated in the brain and sexual glands while BmPcd is expressed in a wider special pattern when the de novo pathway of BH4 is missing
metabolism
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the PCD activity of the homoteterameric enzyme is involved in the aromatic amino acid metabolism
metabolism
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pterin-4a-carbinolamine dehydratase (PCD, BmPcd) and dihydropteridine reductase (DHPR, BmDhpr) might normally act in the regeneration pathway of Bombyx mori
physiological function
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expression of phenylalanine hydroxylase, PhhA (whereby folX and folM are essential for its function), plus the recycling enzyme pterin 4a-carbinolamine dehydratase, PhhB, rescue tyrosine auxotrophy in Escherichia coli
physiological function
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PCD is required for the regeneration of tetrahydrobiopterin after phenylalanine hydroxylation. PCD can dimerize with HNF-1a and work as a transcription factor
physiological function
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pterin-4a-carbinolamine dehydratase regenerates the tetrahydropterin-dependent aromatic amino acid hydroxylase, AAH, tetrahydropterin cofactor from 4a-carbinolamine
physiological function
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pterin-4a-carbinolamine dehydratase regenerates the tetrahydropterin-dependent aromatic amino acid hydroxylase, AAH, tetrahydropterin cofactor from 4a-carbinolamine
physiological function
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the bifunctional protein shows two disparate functions, i.e. dimerization cofactor of HNF-1, DCoH1, and pterin-4a-carbinolamine dehydratase, PCD, that are associated with a change in oligomeric state between dimer and tetramer, overview. The PCD activity of homotetramers aids in aromatic amino acidmetabolism
physiological function
the maize gene Rubisco accumulation factor 2 (raf2) is required for Rubisco biogenesis. RAF2 is conserved among photosynthetic eukaryotes and is related to a mitochondrial protein: dimerization co-factor of hepatocyte nuclear factor 1 (DCoH)/pterin-4a-carbinolamine dehydratases (PCD)-like protein. The pterin-4a-carbinolamine dehydratases (PCD)-like protein RAF2 lacks PCD activity acquires a chloroplast-specific domain. Effect of RAF2 on the accumulation of rbcL and rbcs transcripts is investigated by gel blot analysis of total seedling leaf RNA from wild-type and raf2 mutants
physiological function
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the regeneration pathway (RPB) of tetrahydrobiopterin (BH4), an essential cofactor of aromatic amino acid hydroxylases and nitric oxide synthase playing a key role in many biological processes, in Bombyx mori. The enzyme is involved in the insect BH4 biosynthetic networks, overview
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C81R
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mutant enzyme Cys81Arg has significantly lower activity
E57A
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
E97K
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a biopsy of duodenal mucosa from a patient with homozygous E97K mutation has 17% of normal activity
H61A
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
H61A/H62A
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
H62A
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
H79A
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
H79S
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the His79Ala mutant and the His79Ser mutant exhibit about 40% the activity of the wild-type enzyme. In the mutant enzymes His61Ala and His62Ala the activity is reduced to 10%. In the mutant enzymes Asp60Ala and Arg87Ala the activity is reduced to 30%. The Glu57Ala mutant and the His61Ala,His62Ala double mutant show no activity
N61D
The decreased ability of the N61D mutant to affect HNF1alpha-dependent DNA binding is likely a direct result of altered quaternary structure.
N61D/Q45R/K98Q
site-directed mutagenesis, triple DCoHa mutant (Q45R/K98Q/N61D) is unable to affect HNF1alpha-dependent DNA binding in vitro.
Q45R/K98Q
mutant Q45R/K98Q is not able to affect HNF1alpha-dependent DNA binding in vitro
D100N
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the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
E69A
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the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
H73A
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the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
H73A/H74A
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the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
H74A
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the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
H91A
-
the single mutants H73A and H74A and the double mutant H73A,H74A are completely inactive. The activity of the mutant enzymes H91A and E69A is 40% of the activity of the wild type enzyme. The activity of the mutant enzymes D100N is 10% of the activity of the wild type enzyme
H61A
mutant enzyme H61A shows no dehydratase activity with 4a(R)-hydroxy-6(R)-methyltetrahydropterin. Mutant enzyme H79A shows no dehydratase activity with 4a(S)-hydroxy-6(R)-methyltetrahydropterin. The Km-value for 4a(S)-hydroxy-6(R)-methyltetrahydropterin is comparable to the Km-value of the wild type enzyme. The turnover number of the mutant enzyme H62A is 24% of that with the wild type enzyme for the 4a(R),6(S)-isomer and the 4a(S),6(R)-isomer
T51S
-
the point mutation at the enzyme tetramer interface overcomes the dissociation barrier of the homotetramer and increases the interaction with HNF-1alpha. Presence of an ordered water molecule at the tetramer interface, which may destabilize the homotetramer
C82R
-
mutant enzyme C82R reveals 60% decrease in Vmax and a slight decrease in Km-value for 4a-hydroxytetrahydrobiopterin. The susceptibility to proteolysis of mutant C82R, however is markedly increased compared with the wild type enzyme
C82R
-
mutant enzyme expressed as a soluble form has 40% of normal activity
additional information
-
nine different mutations detected in patients with PCD deficiency. All these mutations are associated with a benign form of tetrahydrobiopterin deficiency, characterized by persistent urinary excretion of 7-substituted biopterin (primapterin or primapterinuria) and transient hyperphenylalaninemia. Most of the mutations recognized in patients with PCD deficiency are either a single amino acid change or a stop codon
additional information
3 residues, Asn61, Gln45, and Lys98 in DCoHalpha play a role in oligomeric flexibility, which enables DCoHalpha to more readily interact with HNF1alpha and increase DNA binding
additional information
raf2 mutant phenotype, overview
additional information
-
raf2 mutant phenotype, overview
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