Thiohistidine Biosynthesis
Ergothioneine and ovothiol A are sulfur-containing histidine derivatives produced by microorganisms including Mycobacterium tuberculosis, Trypanosoma cruzi or Erwinia amylovora and may also play important roles in human physiology. Based on our recent identification of thiohistidine biosyn...
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| Format: | Article |
| Language: | deu |
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Swiss Chemical Society
2013-05-01
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| Series: | CHIMIA |
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| Online Access: | https://www.chimia.ch/chimia/article/view/5396 |
| _version_ | 1818296267046912000 |
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| author | Florian P. Seebeck |
| author_facet | Florian P. Seebeck |
| author_sort | Florian P. Seebeck |
| collection | DOAJ |
| description |
Ergothioneine and ovothiol A are sulfur-containing histidine derivatives produced by microorganisms including Mycobacterium tuberculosis, Trypanosoma cruzi or Erwinia amylovora and may also play important roles in human physiology. Based on our recent identification
of thiohistidine biosynthetic enzymes from Mycobacterium smegmatis and Erwinia tasmaniensis we investigate several aspects of sulfur-based redox biochemistry. For example, we are characterizing the catalytic mechanism of two thiohistidine biosynthetic enzymes which afford O2-dependent
sulfur insertion into the C(5)–H and C(2)–H bonds of the imidazolyl side chain of histidine.
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| first_indexed | 2024-12-13T04:00:49Z |
| format | Article |
| id | doaj.art-553d21c0f79545a5aaf31d0e2c683654 |
| institution | Directory Open Access Journal |
| issn | 0009-4293 2673-2424 |
| language | deu |
| last_indexed | 2024-12-13T04:00:49Z |
| publishDate | 2013-05-01 |
| publisher | Swiss Chemical Society |
| record_format | Article |
| series | CHIMIA |
| spelling | doaj.art-553d21c0f79545a5aaf31d0e2c6836542022-12-22T00:00:27ZdeuSwiss Chemical SocietyCHIMIA0009-42932673-24242013-05-0167510.2533/chimia.2013.333Thiohistidine BiosynthesisFlorian P. Seebeck0University of Basel Department of Chemistry St. Johanns-Ring 19 CH-4056 Basel, Switzerland. florian.seebeck@unibas.ch Ergothioneine and ovothiol A are sulfur-containing histidine derivatives produced by microorganisms including Mycobacterium tuberculosis, Trypanosoma cruzi or Erwinia amylovora and may also play important roles in human physiology. Based on our recent identification of thiohistidine biosynthetic enzymes from Mycobacterium smegmatis and Erwinia tasmaniensis we investigate several aspects of sulfur-based redox biochemistry. For example, we are characterizing the catalytic mechanism of two thiohistidine biosynthetic enzymes which afford O2-dependent sulfur insertion into the C(5)–H and C(2)–H bonds of the imidazolyl side chain of histidine. https://www.chimia.ch/chimia/article/view/5396BiosynthesisErgothioneineOvothiolOxidative stress |
| spellingShingle | Florian P. Seebeck Thiohistidine Biosynthesis CHIMIA Biosynthesis Ergothioneine Ovothiol Oxidative stress |
| title | Thiohistidine Biosynthesis |
| title_full | Thiohistidine Biosynthesis |
| title_fullStr | Thiohistidine Biosynthesis |
| title_full_unstemmed | Thiohistidine Biosynthesis |
| title_short | Thiohistidine Biosynthesis |
| title_sort | thiohistidine biosynthesis |
| topic | Biosynthesis Ergothioneine Ovothiol Oxidative stress |
| url | https://www.chimia.ch/chimia/article/view/5396 |
| work_keys_str_mv | AT florianpseebeck thiohistidinebiosynthesis |