Crystallization (Comment) | Organism |
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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 | Escherichia coli |
Protein Variants | Comment | Organism |
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C27A | significant decrease in catalytic activity | Escherichia coli |
F55L | mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity | Escherichia coli |
W51M | mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity | Escherichia coli |
W51M/F55L | mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | P65870 | - |
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