دورية أكاديمية
In Vitro Reconstitution of a Five-Step Pathway for Bacterial Ergothioneine Catabolism.
| العنوان: | In Vitro Reconstitution of a Five-Step Pathway for Bacterial Ergothioneine Catabolism. |
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| المؤلفون: | Beliaeva MA; Department of Chemistry, University of Basel, Mattenstrasse 24a, Basel 4002, Switzerland., Leisinger F; Department of Chemistry, University of Basel, Mattenstrasse 24a, Basel 4002, Switzerland., Seebeck FP; Department of Chemistry, University of Basel, Mattenstrasse 24a, Basel 4002, Switzerland. |
| المصدر: | ACS chemical biology [ACS Chem Biol] 2021 Feb 19; Vol. 16 (2), pp. 397-403. Date of Electronic Publication: 2021 Feb 05. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, D.C. : American Chemical Society, c2006- |
| مواضيع طبية MeSH: | Bacterial Proteins/*metabolism , Carbon-Nitrogen Lyases/*metabolism , Carbon-Oxygen Lyases/*metabolism , Carbon-Sulfur Lyases/*metabolism , Ergothioneine/*metabolism , Hydrolases/*metabolism, Bacterial Proteins/chemistry ; Biocatalysis ; Carbon-Nitrogen Lyases/chemistry ; Carbon-Oxygen Lyases/chemistry ; Carbon-Sulfur Lyases/chemistry ; Hydrolases/chemistry ; Paenibacillus/metabolism ; Secondary Metabolism ; Substrate Specificity |
| مستخلص: | Ergothioneine is a histidine-derived sulfur metabolite that is biosynthesized by bacteria and fungi. Plants and animals absorb ergothioneine as a micronutrient from their environment or nutrition. Several different mechanisms of microbial ergothioneine production have been described in the past ten years. Much less is known about the genetic and structural basis for ergothioneine catabolism. In this report, we describe the in vitro reconstitution of a five-step pathway that degrades ergothioneine to l-glutamate, trimethylamine, hydrogen sulfide, carbon dioxide, and ammonia. The first two steps are catalyzed by the two enzymes ergothionase and thiourocanate hydratase. These enzymes are closely related to the first two enzymes in histidine catabolism. However, the crystal structure of thiourocanate hydratase from the firmicute Paenibacillus sp. reveals specific structural features that strictly differentiate the activity of this enzyme from that of urocanate hydratases. The final two steps are catalyzed by metal-dependent hydrolases that share most homology with the last two enzymes in uracil catabolism. The early and late part of this pathway are connected by an entirely new enzyme type that catalyzes desulfurization of a thiohydantoin intermediate. Homologous enzymes are encoded in many soil-dwelling firmicutes and proteobacteria, suggesting that bacterial activity may have a significant impact on the environmental availability of ergothioneine. |
| المشرفين على المادة: | 0 (Bacterial Proteins) BDZ3DQM98W (Ergothioneine) EC 3.- (Hydrolases) EC 4.2.- (Carbon-Oxygen Lyases) EC 4.3.- (Carbon-Nitrogen Lyases) EC 4.4.- (Carbon-Sulfur Lyases) |
| تواريخ الأحداث: | Date Created: 20210205 Date Completed: 20210628 Latest Revision: 20210628 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1021/acschembio.0c00968 |
| PMID: | 33544568 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1554-8937 |
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| DOI: | 10.1021/acschembio.0c00968 |