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Information on EC 4.2.1.96 - 4a-hydroxytetrahydrobiopterin dehydratase and Organism(s) Mus musculus and UniProt Accession Q9CZL5

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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-1alpha (HNF-1).
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Mus musculus
UNIPROT: Q9CZL5
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DcoH2
dimerization cofactor of HNF1alpha
4 alpha-Hydroxy-tetrahydropterin dehydratase
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4-alpha-hydroxy-tetrahydropterin dehydratase
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4a-Carbinolamine dehydratase
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4a-Hydroxytetrahydrobiopterin dehydratase
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4a-Hydroxytetrahydropterin dehydratase
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cDcoH
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DCoH
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-
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DCoH/PCD
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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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P4aCD
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PCD
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PCD/DCoH
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PCD/PhhB
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PCDH
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Phenylalanine hydroxylase-stimulating protein
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Phenylalanine hydroxylase-stimulating protein/pterin-4alpha-carbinolamine dehydratase
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PHS
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PHS/PCD
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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
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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
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Pterin-4alpha-carbinolamine dehydratase (PCD)/dimerization cofactor for the transcription factor HBF-1alpha
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XDCoH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of H2O
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PATHWAY SOURCE
PATHWAYS
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
204788-56-7
pterin-4a-carbinolamine dehydratase (Aquifex aeolicus gene phhB), genBank AE000671-derived protein GI 2982796
87683-70-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DcoH2 (dimerization cofactor of HNF1alpha)
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHS2_MOUSE
136
0
14830
Swiss-Prot
Mitochondrion (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
DcoH2 (dimerization cofactor of HNF1alpha), forms a tetramer, readily disproportionates and forms a 2:2 complex with HNF1 in vitro
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method at 4°C, 1.6 A resolution crystal structure, space group P3(1)21, unit cell length: a = b = 57.92 A, c = 114.63 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DcoH2 (dimerization cofactor of HNF1alpha)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rose, R.B.; Pullen, K.E.; Bayle, J.H.; Crabtree, G.R.; Alber, T.
Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2
Biochemistry
43
7345-7355
2004
Mus musculus (Q9CZL5)
Manually annotated by BRENDA team