Isolation and characterization of the Drosophila melanogaster cDNA encoding the sepiapterin reductase.
We have isolated and characterized the cDNA encoding Drosophila melanogaster sepiapterin reductase (SR). The amino acid sequence deduced from the cDNA sequence was 29% identical to those of mammalian SRs. The active site residues proposed from the three-dimensional structure of mouse SR are well conserved in Drosophila SR. The protein-coding region of the cDNA was expressed in Escherichia coli as a histidine fusion protein, and the resulting recombinant protein proved to have SR activity. The SR activity of the recombinant protein was inhibited by two indoleamines, N-acetyl serotonin and melatonin. Southern analysis suggests that the Drosophila SR gene is encoded by a single copy gene. RNA blot analysis revealed that the gene expresses 1.5 kb mRNA in both adult heads and bodies.
Seong
C
C
Department and Institute of Genetic Engineering, Kyung Hee University, Yongin City 449-701, South Korea.
Kim
Y A
YA
Chung
H J
HJ
Park
D
D
Yim
J
J
Baek
K
K
Park
Y S
YS
Han
K
K
Yoon
J
J
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry / Q000302:isolation & purification; D004331:Drosophila melanogaster / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics; D016415:Sequence Alignment
D018076:DNA, Complementary; D012333:RNA, Messenger; D000429:Alcohol Oxidoreductases; C022630:sepiapterin reductase