Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System
Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutat...
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MDPI AG
2020-05-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/6/826 |
| _version_ | 1797566812851798016 |
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| author | Noriyuki Nagahara |
| author_facet | Noriyuki Nagahara |
| author_sort | Noriyuki Nagahara |
| collection | DOAJ |
| description | Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant <i>Escherichia coli</i> glutaredoxin1 (Cys<sup>14</sup> is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase. |
| first_indexed | 2024-03-10T19:32:40Z |
| format | Article |
| id | doaj.art-641502b4165043d7bb0d34f3461e91a1 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T19:32:40Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-641502b4165043d7bb0d34f3461e91a12023-11-20T01:59:42ZengMDPI AGBiomolecules2218-273X2020-05-0110682610.3390/biom10060826Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing SystemNoriyuki Nagahara0Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi Bunkyo-Ku, Tokyo 113-8602, JapanGlutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant <i>Escherichia coli</i> glutaredoxin1 (Cys<sup>14</sup> is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.https://www.mdpi.com/2218-273X/10/6/826glutaredoxinglutathioneglutathione reductase3-mercaptopyruvate sulfurtransferase |
| spellingShingle | Noriyuki Nagahara Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System Biomolecules glutaredoxin glutathione glutathione reductase 3-mercaptopyruvate sulfurtransferase |
| title | Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System |
| title_full | Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System |
| title_fullStr | Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System |
| title_full_unstemmed | Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System |
| title_short | Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System |
| title_sort | activation of 3 mercaptopyruvate sulfurtransferase by glutaredoxin reducing system |
| topic | glutaredoxin glutathione glutathione reductase 3-mercaptopyruvate sulfurtransferase |
| url | https://www.mdpi.com/2218-273X/10/6/826 |
| work_keys_str_mv | AT noriyukinagahara activationof3mercaptopyruvatesulfurtransferasebyglutaredoxinreducingsystem |