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4.2.1.96: 4a-hydroxytetrahydrobiopterin dehydratase

This is an abbreviated version!
For detailed information about 4a-hydroxytetrahydrobiopterin dehydratase, go to the full flat file.

Word Map on EC 4.2.1.96

Reaction

4a-hydroxytetrahydrobiopterin
=
6,7-dihydrobiopterin
 +
H2O

Synonyms

4 alpha-Hydroxy-tetrahydropterin dehydratase, 4-alpha-hydroxy-tetrahydropterin dehydratase, 4-alpha-hydroxytetrahydrobiopterin dehydratase, 4a-Carbinolamine dehydratase, 4a-Hydroxytetrahydrobiopterin dehydratase, 4a-Hydroxytetrahydropterin dehydratase, carbinolamine-4a-dehydratase, cDcoH, DCoH, DCoH/PCD, DcoH2, DCoHalpha, Dehydratase, 4a-carbinolamine, Dimerization cofactor of hepatocyte nuclear factor 1-alpha, Dimerization cofactor of HNF1, Dimerization factor of HNF1/pterin-4alpha-carbinolamine dehydratase, GenBank AE000671-derived protein GI 2982796, More, P4aCD, PCD, PCD/DCoH, PCD/PhhB, PCDH, Phenylalanine hydroxylase-stimulating protein, Phenylalanine hydroxylase-stimulating protein/pterin-4alpha-carbinolamine dehydratase, PhhB, PHS, PHS/PCD, pterin 4a-carbinolamine dehydratase, 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

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.96 4a-hydroxytetrahydrobiopterin dehydratase

Engineering

Engineering on EC 4.2.1.96 - 4a-hydroxytetrahydrobiopterin dehydratase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C81R
-
mutant enzyme Cys81Arg has significantly lower activity
E57A
-
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
-
a biopsy of duodenal mucosa from a patient with homozygous E97K mutation has 17% of normal activity
H61A
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
additional information