Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases

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• 作者：Venkat N. Are^a ; ^c ; ¹ ; Ashwani Kumar^a ; ¹ ; Saurabh Kumar^b ; Venuka Durani Goyal^a ; Biplab Ghosh^a ; Deepak Bhatnagar^c ; Sahayog N. Jamdar^b ; ^{snjam2@gmail.com} ; Ravindra D. Makde^a ; ^{ravimakde@rrcat.gov.in}
• 关键词：XPD ; Xaa-Pro dipeptidase ; XPDxc ; Xaa-Pro dipeptidase from Xanthomonas campestris ; XPDmt ; Xaa-Pro dipeptidase from Mycobacterium tuberculosis ; XPDll ; Xaa-Pro dipeptidase from Lactococcus lactis ; AMPPec ; aminopeptidase P from Escherichia coli ; PDB ; Protein Data Bank
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1865
• 期：2
• 页码：153-164
• 全文大小：2829 K
• 卷排序：1865

文摘

Comprehensive structural & biochemical characterization of bacterial Xaa-Pro dipeptidases Novel mechanism of substrate selectivity and binding Likely structural basis for substrate inhibitions and allosteric behaviour Conserved sequence motifs defines new subfamily in prolidases.