4.1.2.50: 6-carboxytetrahydropterin synthase
This is an abbreviated version!
For detailed information about 6-carboxytetrahydropterin synthase, go to the full flat file.
Word Map on EC 4.1.2.50
Reaction
Synonyms
6-carboxy-5,6,7,8-tetrahydropterin synthase, 6-pyruvoyltetrahydropterin synthase, CPH4 synthase, PTPS, QueD
ECTree
4.1.2.50 6-carboxytetrahydropterin synthaseAdvanced search results
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results (Crystallization
Crystallization on EC 4.1.2.50 - 6-carboxytetrahydropterin synthase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
purified recomb inant QueD, hanging-drop vapor-diffusion method, mixing of 800 nl of protein solution containing 10 mg/ml protein and of 800 nl crystallization solution containing 25% PEG 600, 100 mM NaCl and sodium citrate buffer, pH 5.5, at 18°C, X-ray diffraction structure determination and analysis at 3.6 A resolution
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crystal structures of wild-type apo 6-carboxytetrahydropterin synthase and of a C27A mutant complexed with sepiapterin to 2.3 and 2.5 A resolution, respectively. The structures are highly conserved at the active site and the Zn2+ binding site. Residues Trp51 and Phe55, that are not found in mammalian 6-pyruvoyltetrahydropterin synthase keep the substrate bound by stacking it with their side chains. Replacement of these two residues by site-directed mutagenesis to the residues Met and Leu, which are only found in mammalian 6-pyruvoyltetrahydropterin synthase, converted the enzyme to the mammalian 6-pyruvoyltetrahydropterin synthase activity
hanging drop vapor diffusion method, using 5% (v/v) 2-methyl-1,3-propanediol, 0.04 M CaCl2, 0.1 M sodium acetate (pH 4.5)
