4.2.1.96	C81R	mutant enzyme Cys81Arg has significantly lower activity	5932	
4.2.1.96	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	5936	
4.2.1.96	C82R	mutant enzyme expressed as a soluble form has 40% of normal activity	668883	
4.2.1.96	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	5929	
4.2.1.96	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	5933	
4.2.1.96	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	5929	
4.2.1.96	E97K	a biopsy of duodenal mucosa from a patient with homozygous E97K mutation has 17% of normal activity	668883	
4.2.1.96	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	5940	
4.2.1.96	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	5933	
4.2.1.96	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	5933	
4.2.1.96	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	5933	
4.2.1.96	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	5929	
4.2.1.96	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	5929	
4.2.1.96	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	5929	
4.2.1.96	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	5933	
4.2.1.96	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	5933	
4.2.1.96	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	5929	
4.2.1.96	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	690623	
4.2.1.96	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	668883	
4.2.1.96	additional information	raf2 mutant phenotype, overview	748945	
4.2.1.96	N61D	The decreased ability of the N61D mutant to affect HNF1alpha-dependent DNA binding is likely a direct result of altered quaternary structure.	690623	
4.2.1.96	N61D/Q45R/K98Q	site-directed mutagenesis, triple DCoHa mutant (Q45R/K98Q/N61D) is unable to affect HNF1alpha-dependent DNA binding in vitro.	690623	
4.2.1.96	Q45R/K98Q	mutant Q45R/K98Q is not able to affect HNF1alpha-dependent DNA binding in vitro	690623	
4.2.1.96	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	714176