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Information on EC 4.2.1.96 - 4a-hydroxytetrahydrobiopterin dehydratase
for references in articles please use BRENDA:EC4.2.1.96
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EC Tree 4 Lyases
4.2 Carbon-oxygen lyases
4.2.1 Hydro-lyases
4.2.1.96 4a-hydroxytetrahydrobiopterin dehydratase
IUBMB Comments
In concert with EC 1.5.1.34, 6,7-dihydropteridine reductase, the enzyme recycles 4a-hydroxytetrahydrobiopterin back to tetrahydrobiopterin, a cosubstrate for several enzymes, including aromatic amino acid hydroxylases. The enzyme is bifunctional, and also acts as a dimerization cofactor of hepatocyte nuclear factor-1α (HNF-1).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 4.2.1.96
- pterins
- hyperphenylalaninemias
- dihydropteridine
- bh4
- hydroxylases
-
cyclohydrolase
-
7-biopterin
- 6-pyruvoyl-tetrahydropterin
- vitiligo
-
hnf1alpha
- sepiapterin
- tetrahydropterins
-
depigmentation
- gtpch
Reaction Schemes
show=
6,7-dihydrobiopterin
+
Synonyms
pcd/dcoh, pterin-4a-carbinolamine dehydratase, dcoh/pcd, dcoh2, dcohalpha, xdcoh, 4a-carbinolamine dehydratase, pterin-4alpha-carbinolamine dehydratase, pterin-4 alpha-carbinolamine dehydratase, cdcoh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4 alpha-Hydroxy-tetrahydropterin dehydratase
-
-
-
-
4-alpha-hydroxy-tetrahydropterin dehydratase
-
-
-
-
4a-Carbinolamine dehydratase
-
-
-
-
4a-Hydroxytetrahydrobiopterin dehydratase
4a-Hydroxytetrahydropterin dehydratase
-
-
-
-
cDcoH
-
-
-
-
DCoH
-
-
-
-
DCoH/PCD
-
-
-
-
DCoHalpha
Dehydratase, 4a-carbinolamine
-
-
-
-
Dimerization cofactor of hepatocyte nuclear factor 1-alpha
-
-
-
-
Dimerization cofactor of HNF1
-
-
-
-
Dimerization factor of HNF1/pterin-4alpha-carbinolamine dehydratase
-
-
-
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GenBank AE000671-derived protein GI 2982796
-
-
-
-
P4aCD
-
-
-
-
PCD
PCD/DCoH
PCD/PhhB
-
-
-
-
PCDH
-
-
-
-
Phenylalanine hydroxylase-stimulating protein
-
-
-
-
Phenylalanine hydroxylase-stimulating protein/pterin-4alpha-carbinolamine dehydratase
-
-
-
-
PHS
-
-
-
-
PHS/PCD
-
-
-
-
Pterin carbinolamine dehydratase
-
-
-
-
Pterin-4 alpha-carbinolamine dehydratase
-
-
-
-
Pterin-4-alpha-carbinolamine dehydratase
-
-
-
-
Pterin-4a-carbinolamine dehydratase
Pterin-4a-carbinolamine dehydratase (Aquifex aeolicus gene phhB)
-
-
-
-
Pterin-4a-carbinolamine dehydratase/dimerization cofactor of HNF1
-
-
-
-
Pterin-4alpha-carbinolamine dehydratase
Pterin-4alpha-carbinolamine dehydratase (PCD)/dimerization cofactor for the transcription factor HBF-1alpha
-
-
-
-
XDCoH
-
-
-
-
additional information
4a-Hydroxytetrahydrobiopterin dehydratase
-
-
-
-
PCD
-
-
-
-
PCD/DCoH
-
-
-
-
Pterin-4a-carbinolamine dehydratase
-
-
-
-
Pterin-4alpha-carbinolamine dehydratase
-
-
-
-
additional information
-
the enzyme has identical amino acid sequence to DCoH, the dimerization cofactor of the transcription regulator, HNF-1alpha
additional information
-
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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H2O
-
-
-
-
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H2O
the mechanism of dehydration involves base catalysis at the N(5)-H group of the substrate by His61
-
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H2O
His61 and His79 act as acid catalysts for the stereospecific elimination of the 4a(R)- and 4a(S)-hydroxyl groups, respectively. The role of His62 is primarily binding substrate with additional component of base catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination of H2O
elimination of H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
L-phenylalanine degradation V, tetrahydropteridine recycling
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SYSTEMATIC NAME
IUBMB Comments
4a-hydroxytetrahydrobiopterin hydro-lyase (6,7-dihydrobiopterin-forming)
In concert with EC 1.5.1.34, 6,7-dihydropteridine reductase, the enzyme recycles 4a-hydroxytetrahydrobiopterin back to tetrahydrobiopterin, a cosubstrate for several enzymes, including aromatic amino acid hydroxylases. The enzyme is bifunctional, and also acts as a dimerization cofactor of hepatocyte nuclear factor-1alpha (HNF-1).
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CAS REGISTRY NUMBER
COMMENTARY
204788-56-7
pterin-4a-carbinolamine dehydratase (Aquifex aeolicus gene phhB), genBank AE000671-derived protein GI 2982796
87683-70-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
Substrates: -
Products: -
Products: -
?
4a(R)-hydroxy-6(S)-propyltetrahydropterin
quinoid 6(S)-propyldihydropterin
-
Substrates: -
Products: -
Products: -
?
4a(S)-hydroxy-6(R)-methyltetrahydropterin
quinoid 6(R)-methyldihydropterin
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(R)-dihydroxypropyltetrahydropterin
?
-
Substrates: -
Products: -
Products: -
?
4a-hydroxy-tetrahydrobiopterin
7,8-dihydrobiopterin + H2O
-
Substrates: -
Products: -
Products: -
?
6(S)-methyl-4a-hydroxy-tetrahydropterin
6(S)-methyl-7,8-dihydropterin + H2O
-
Substrates: -
Products: -
Products: -
?
6,6-dimethyl-4a-hydroxy-tetrahydropterin
6,6-dimethyl-7,8-dihydropterin + H2O
-
Substrates: -
Products: -
Products: -
?
pterin-4alpha-carbinolamine
quininoid dihydropterin + H2O
-
Substrates: -
Products: -
Products: -
?
(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
-
Substrates: -
Products: -
Products: -
?
(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
Substrates: -
Products: -
Products: -
?
(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
-
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
-
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
-
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(S)-methyltetrahydropterin
Quinoid 6(S)-methyldihydropterin
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(S)-propyltetrahydropterin
Quinoid 6(S)-propyldihydropterin
-
Substrates: -
Products: -
Products: -
?
4a-Hydroxy-6(S)-propyltetrahydropterin
Quinoid 6(S)-propyldihydropterin
-
Substrates: -
Products: -
Products: -
?
4a-hydroxy-tetrahydropterin
7,8-dihydropterin + H2O
-
Substrates: -
Products: -
Products: -
?
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
?
-
Substrates: -
Products: -
Products: -
?
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: a defect in 4a-hydroxytetrahydrobiopterin dehydratase provoces the conversion of the 6-substituted pterins to their 7-substituted isomers
Products: -
Products: -
?
additional information
?
-
-
Substrates: the mutant enzyme form C82R and the 18-amino acid-truncated mutant Glu87-termination occur naturally associated with hyperphenyalaninemia
Products: -
Products: -
?
additional information
?
-
-
Substrates: the codevelopment of 4a-hydroxytetrahydropterin dehydratase with dihydropteridine reductase strongly supports a physiologically significant role for the dehydratase in tetrahydrobiopterin regeneration
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: DCoHalpha is coactivator of HNF1alpha-depndent transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a role in the regulation of expression of phenylalanine hydroxylase via transcription factor HNF1alpha
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: a defect in 4a-hydroxytetrahydrobiopterin dehydratase provoces the conversion of the 6-substituted pterins to their 7-substituted isomers
Products: -
Products: -
?
additional information
?
-
-
Substrates: the mutant enzyme form C82R and the 18-amino acid-truncated mutant Glu87-termination occur naturally associated with hyperphenyalaninemia
Products: -
Products: -
?
additional information
?
-
-
Substrates: the codevelopment of 4a-hydroxytetrahydropterin dehydratase with dihydropteridine reductase strongly supports a physiologically significant role for the dehydratase in tetrahydrobiopterin regeneration
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme is involved in the regeneration of tetrahydrobiopterin, the cofactor of aromatic amino acid monooxygenases
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essentially identical to a cofactor that regulates dimerization of a nuclear homeodomain-containing protein involved in transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a role in the regulation of expression of phenylalanine hydroxylase via transcription factor HNF1alpha
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyldicarbonate
inactivation is complete when about 1.2 His per subunit are derivatized
glycerol
-
dietary glycerol leads to a small reduction in the mRNA level of the enzyme PCD/DCoH only in the liver, not in kidney, 40% glycerol diet lead to 2.5fold reduced activity in liver cytosol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
-
leads to a slight increase in enzyme activity only in the kidney, not in liver, when feeded as a 40% glycerol diet
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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.
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
Suspected pterin-4a-carbinolamine dehydratase deficiency: hyperphenylalaninaemia due to inhibition of phenylalanine hydroxylase by tetrahydro-7-biopterin.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.02
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
-
wild type enzyme and mutant enzyme G72D
0.025
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
-
mutant enzyme E69A
0.06
6(S)-methyl-7,8-dihydropterin-4a-carbinolamine
-
mutant enzyme H91A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
N61D
23
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
N61D/Q45R/K98Q
23
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
Q45R/K98Q
24
(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin
wild-type
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type and mutant enzymes E57A, H61A, H62A, H79A, Y69F, and D60A and double-mutant H61A,H62A expressed in Escherichia coli
-
-
brenda
wild type and mutant enzymes E69A, D100N, H73A, H74A, H73A,H74A, H91A, W81A, and G72S expressed in Escherichia coli
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
PCD enzyme transcription profiles in different strains, expression analysis, overview. BmPcd is expressed almost throughout the whole life cycle
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
co-localization and complex formation with aromatic amino acid hydroxylase, AAH, overview
brenda
-
co-localization and complex formation with aromatic amino acid hydroxylase, AAH, overview
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
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
-
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
-
the PCD activity of the homoteterameric enzyme is involved in the aromatic amino acid metabolism
metabolism
-
pterin-4a-carbinolamine dehydratase (PCD, BmPcd) and dihydropteridine reductase (DHPR, BmDhpr) might normally act in the regeneration pathway of Bombyx mori
physiological function
-
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
-
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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