The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies
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- 作者：Andrea Picaa ; b ; Meng-Chun Chic ; Yi-Yu Chenc ; Marco d'Ischiaa ; Long-Liu Linc ; Antonello Merlinoa ; b ; antonello.merlino@unina.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：BlGT ; γ-Glutamyl transpeptidase from Bacillus licheniformis ; BpGT ; γ-Glutamyl transpeptidase from Bacillus pumilus ; BsGT ; γ-Glutamyl transpeptidase from Bacillus subtilis ; EcGT ; γ-Glutamyl transpeptidase from E. coli ; GSH ; γ-Glutamyl-cysteinyl-glycine ; GtGT ; γ-Glutamyl transpeptidase from Geobacillus thermodenitrificans ; hGT ; Human γ-glutamyl transpeptidase ; HpGT ; γ-Glutamyl transpeptidase from Helicobacter pylori ; Ntn ; N-terminal nucleophile ; γ-GTs ; γ-Glutamyl transpeptidases
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：1864
- 期：2
- 页码：195-203
- 全文大小：1508 K
文摘
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X-ray structure of the precursor mimic of BlGT was solved.
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X-ray Structure highlights a number of residues that are crucial for autoprocessing.
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Mutation of H401, T415, T417, E419 and R571 decelerate BlGT autoprocessing.
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A possible mechanism of gamma-GT autoprocessing is proposed.