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Structure of Bacillus subtilis γ-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue
γ-Glutamyltranspeptidase (GGT) is an enzyme that plays a central role in glutathione metabolism, and acivicin is a classical inhibitor of GGT. Here, the structure of acivicin bound to Bacillus subtilis GGT determined by X-ray crystallography to 1.8 Å resolution is presented, in which it binds to the...
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| Main Authors: | , , , , |
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| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
International Union of Crystallography
2014
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3940202/ https://ncbi.nlm.nih.gov/pubmed/24531494 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004713031222 |
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