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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Hlavní autoři: Ida, Tomoyo, Suzuki, Hideyuki, Fukuyama, Keiichi, Hiratake, Jun, Wada, Kei
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2014
Témata:
Research Papers
On-line přístup: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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