Cloning and sequencing of a human thioredoxin reductase.
The DNA sequence encoding human placental thioredoxin reductase has been determined. Of the 3826 base pairs sequenced, 1650 base pairs were in an open reading frame encoding a mature protein with 495 amino acids and a calculated molecular mass of 54,171. Sequence analysis showed strong similarity to glutathione reductases and other NADPH-dependent reductases. Human thioredoxin reductase contains the redox-active cysteines in the putative FAD binding domain and has a dimer interface domain not previously seen with prokaryote and lower eukaryote thioredoxin reductases.
Gasdaska
P Y
PY
Arizona Cancer Center, Tucson 85724, USA.
Gasdaska
J R
JR
Cochran
S
S
Powis
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001482:Base Composition; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005260:Female; D005980:Glutathione Reductase / Q000235:genetics; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides; D016366:Open Reading Frames; D010920:Placenta / Q000201:enzymology*; D010944:Plants / Q000201:enzymology; D011247:Pregnancy; D017386:Sequence Homology, Amino Acid; D013880:Thioredoxin-Disulfide Reductase / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification
D009838:Oligodeoxyribonucleotides; D005980:Glutathione Reductase; D013880:Thioredoxin-Disulfide Reductase