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Results 1 - 10 of 27 > >>
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153D257H mutant shows completely inhibited sepiapterin reduction. Mutation has only minimal effects on redox cycling 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153DELTA257-261 deletion of the C-terminal 5 amino acids almost completely eliminates enzyme activity. For redox cycling, the catalytic efficacy decreases to less than 1% of the wild type enzyme 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153F99A the mutant shows 3.9fold higher Km and lower Vmax (8.95%) than the wild type enzyme 695294
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153G14S mutations in Gly14 and Gly18 in the NADPH binding motif of sepiapterin reductase results in almost complete loss of the ability to reduce sepiapterin, and a 65-75% decrease in redox cycling. For both of these mutations, the catalytic efficiencies for redox cycling decreases to 0.2% of wild type sepiapterin reductase 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153G18D mutations in Gly14 and Gly18 in the NADPH binding motif of sepiapterin reductase results in almost complete loss of the ability to reduce sepiapterin, and a 65-75% decrease in redox cycling. For both of these mutations, the catalytic efficiencies for redox cycling decreases to 0.2% of wild type sepiapterin reductase 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153K174L catalytic efficiencies (Kcat/Km) for sepiapterin reduction of S157A mutant and K174L mutant decreases to 1.8% and 0.8% of wild type sepiapterin reductase, respectively, and for redox cycling to 6.8% and 1.4%, respectively 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153K175I decreased activity against a pteridine substrate and exogenous carbonyl compound 286028
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153K251X naturally occurring mutation in gene SPR, exon 3, causing enzyme deficiency 668883
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153M205G mutation leads to marked reductions in the activities of both sepiapterin reduction and redox cycling. The catalytic efficiency of N99A and M205G for sepiapterin reduction decreases to approximately 1% and 5%, respectively, and for redox cycling, 5% and 25%, respectively, when compared to the wild type enzyme 725527
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.153more a single nucleotide polymorphism around the SPR gene is involved in development of Parkonson's disease 685875
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