TY - JOUR
T1 - Delivery of selenium to selenophosphate synthetase for selenoprotein biosynthesis
AU - Tobe, Ryuta
AU - Mihara, Hisaaki
N1 - Funding Information:
This study was supported by the Program for the Third-Phase R-GIRO Research (to Hisaaki Mihara) from the Ritsumeikan Global Innovation Research Organization, Ritsumeikan University , by a Grant-in-Aid for Scientific Research (B) 16H04913 (to Hisaaki Mihara) from JSPS, and a Grant-in-Aid for Young Scientists (B) 16 K18691 (to Ryuta Tobe) from JSPS.
Funding Information:
This study was supported by the Program for the Third-Phase R-GIRO Research (to Hisaaki Mihara) from the Ritsumeikan Global Innovation Research Organization, Ritsumeikan University, by a Grant-in-Aid for Scientific Research (B) 16H04913 (to Hisaaki Mihara) from JSPS, and a Grant-in-Aid for Young Scientists (B) 16?K18691 (to Ryuta Tobe) from JSPS.
Publisher Copyright:
© 2018 Elsevier B.V.
PY - 2018/11
Y1 - 2018/11
N2 - Background: Selenophosphate, the key selenium donor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H2O. Although free selenide can be used as the in vitro selenium substrate for selenophosphate synthesis, the precise physiological system that donates in vivo selenium substrate to SPS has not yet been characterized completely. Scope of review: In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. Major conclusions: Glutathione, selenocysteine lyase, cysteine desulfurase, and selenium-binding proteins are the candidates of selenium delivery system to SPS. The thioredoxin system is also implicated in the selenium delivery to SPS in Escherichia coli. General significance: Selenium delivered via a protein-bound selenopersulfide intermediate emerges as a central element not only in achieving specific selenoprotein biosynthesis but also in preventing the occurrence of toxic free selenide in the cell. This article is part of a Special Issue entitled “Selenium research in biochemistry and biophysics – 200 year anniversary”.
AB - Background: Selenophosphate, the key selenium donor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H2O. Although free selenide can be used as the in vitro selenium substrate for selenophosphate synthesis, the precise physiological system that donates in vivo selenium substrate to SPS has not yet been characterized completely. Scope of review: In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. Major conclusions: Glutathione, selenocysteine lyase, cysteine desulfurase, and selenium-binding proteins are the candidates of selenium delivery system to SPS. The thioredoxin system is also implicated in the selenium delivery to SPS in Escherichia coli. General significance: Selenium delivered via a protein-bound selenopersulfide intermediate emerges as a central element not only in achieving specific selenoprotein biosynthesis but also in preventing the occurrence of toxic free selenide in the cell. This article is part of a Special Issue entitled “Selenium research in biochemistry and biophysics – 200 year anniversary”.
KW - Selenide
KW - Selenium delivery protein
KW - Selenium metabolism
KW - Selenopersulfide
KW - Selenophosphate synthetase
KW - Selenoprotein biosynthesis
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U2 - 10.1016/j.bbagen.2018.05.023
DO - 10.1016/j.bbagen.2018.05.023
M3 - Review article
C2 - 29859962
AN - SCOPUS:85048516219
SN - 0006-3002
VL - 1862
SP - 2433
EP - 2440
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 11
ER -