• SepiapterinReductase
• References
• Slides

1) Protein identification and analysis tools on the ExPASy server. Gasteiger, E. et. al. In J. M. Walker (Ed.) The proteomics protocols handbook. Totowa, New Jersey: Humana Press Inc. 2005.

2) Fujimoto, K., Hara, M., Yamada, H., Sakurai, M., Inaba, A., Tomomura, A., and Katoh, S., 2001. Role of the conserved Ser-Tyr-Lys triad of the SDR family in sepiapterin reductase. Chemico-Biological Interactions 130-132: 825-832.

3) Fujimoto, K., Ichinose, H., Nagatsu, T., Nonaka, T., Mitsui, Y., and Katoh, S., 1999. Functionally important residues tyrosine-171 and serine-158 in sepiapterin reductase. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology 1431: 306-314. 

4) Haruki, H., Pederson, M.G., Gorska, K.I., Pojer, F., and Johnsson, K., 2013. Tetrahydrobiopterin biosynthesis as an off-target of sulfa drugs. Science 340: 987-991. 

5) Aerbach, G., Herrman, A., Gütlich, M., Fischer, M., Jacob, U., Bacher, A., and Huber, R., 1997. The 1.24 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. The EMBO Journal 16: 7219-7230. 

6) Dali server: conservation mapping in 3D. Nucl. Acids Res. 38, W545-549. Holm L, Rosenström, P. 2010.

7) Protein Data Bank. http://pdb.org/pdb/home/home.do.

8) Ota, A., Ichinose, H., and Nagatsu, T., 1995. Mouse sepiapterin reductase: an enzyme involved in the final step of tetrabiopterin biosynthesis. Primary structure deduced from the cDNA sequence. Biochimica et Biophysica Acta 1260: 320-322. 

9) BLAST: Basic Local Alignment Search Tool.  http://www.ncbi.nlm.nih.gov/blast/Blast.cgi.