Sequence of SPRE_RAT
EC Number:1.1.1.153
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
P18297
Rattus norvegicus
262
28128
Reaction
L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
Other sequences found for EC No. 1.1.1.153
General information:
Sequence
0 MEGGRLGCAV CVLTGASRGF GRALAPQLAG LLSPGSVLLL SARSDSMLRQ LKEELCTQQP
60 GLQVVLAAAD LGTESGVQQL LSAVRELPRP ERLQRLLLIN NAGTLGDVSK GFLNINDLAE
120 VNNYWALNLT SMLCLTTGTL NAFSNSPGLS KTVVNISSLC ALQPFKGWGL YCAGKAARDM
180 LYQVLAVEEP SVRVLSYAPG PLDTNMQQLA RETSMDPELR SRLQKLNSEG ELVDCGTSAQ
240 KLLSLLQRDT FQSGAHVDFY DI
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
739539
Citron B.A.,Milstien S.,Gutierrez J.C.,Levine R.A.,Yanak B.L.,Kaufman S.
Isolation and expression of rat liver sepiapterin reductase cDNA.
Proc. Natl. Acad. Sci. U.S.A.
87
6436-6440
1990
739540
Oyama R.,Katoh S.,Sueoka T.,Suzuki M.,Ichinose H.,Nagatsu T.,Titani K.
The complete amino acid sequence of the mature form of rat sepiapterin reductase.
Biochem. Biophys. Res. Commun.
173
627-631
1990
739541
Fujimoto K.,Ichinose H.,Nagatsu T.,Nonaka T.,Mitsui Y.,Katoh S.
Functionally important residues tyrosine-171 and serine-158 in sepiapterin reductase.
Biochim. Biophys. Acta
1431
306-314
1999
739542
Fujimoto K.,Takahashi S.Y.,Katoh S.
Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II.
Biochim. Biophys. Acta
1594
191-198
2002
739543
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
