Delivery of selenium to selenophosphate synthetase for selenoprotein biosynthesis
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 physiol...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1862; no. 11; pp. 2433 - 2440 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.11.2018
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| Subjects | |
| Online Access | Get full text |
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| Abstract | 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.
In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis.
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.
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”.
[Display omitted]
•Selenophosphate is synthesized from selenide by selenophosphate synthetase (SPS).•Free selenide is rarely present in cells, as it is highly reactive and cytotoxic.•Selenium is delivered to SPS by selenium delivery proteins and thiol compounds.•Thioredoxin system is implicated in selenium delivery to SPS in Escherichia coli. |
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| AbstractList | 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.BACKGROUNDSelenophosphate, 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.In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis.SCOPE OF REVIEWIn this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis.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.MAJOR CONCLUSIONSGlutathione, 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.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".GENERAL SIGNIFICANCESelenium 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". 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.In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis.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.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”. 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. In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. 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. 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”. [Display omitted] •Selenophosphate is synthesized from selenide by selenophosphate synthetase (SPS).•Free selenide is rarely present in cells, as it is highly reactive and cytotoxic.•Selenium is delivered to SPS by selenium delivery proteins and thiol compounds.•Thioredoxin system is implicated in selenium delivery to SPS in Escherichia coli. Selenophosphate, the key selenium donor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H O. 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. In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. 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. 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". |
| Author | Tobe, Ryuta Mihara, Hisaaki |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29859962$$D View this record in MEDLINE/PubMed |
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| Keywords | Selenide EcSPS O2 Selenopersulfide CysDS GSSeH Grx Sec GSSeSG Selenoprotein biosynthesis SPS SeM Selenophosphate synthetase Selenium metabolism SCLY Trx GSH Selenium delivery protein Se0 TrxR |
| Language | English |
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| SubjectTerms | adenosine triphosphate biophysics biosynthesis cysteine Escherichia Selenide selenium Selenium delivery protein Selenium metabolism selenocysteine Selenopersulfide Selenophosphate synthetase Selenoprotein biosynthesis selenoproteins thioredoxins toxicity transfer RNA |
| Title | Delivery of selenium to selenophosphate synthetase for selenoprotein biosynthesis |
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