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Literature summary for 4.1.2.50 extracted from

  • Seo, K.H.; Zhuang, N.; Park, Y.S.; Park, K.H.; Lee, K.H.
    Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity (2014), Acta Crystallogr. Sect. D, 70, 1212-1223.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Escherichia coli P65870
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