期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 468, 期 2, 页码 217-225出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.09.023
关键词
peptide deformylase; hydrolase; iron; zinc; metal specificity; catalysis
资金
- NIAID NIH HHS [R01 AI062901, R01 AI040575-09, R01 AI062901-03, R01 AI040575, AI62901, AI40575] Funding Source: Medline
Peptide deformylase (PDF, E.C. 3.5.1.88) catalyzes the removal of N-terminal formyl groups from nascent ribosome-synthesized polypeptides. PDF contains a catalytically essential divalent metal ion, which is tetrahedrally coordinated by three protein ligands (His, His, and Cys) and a water molecule. Previous studies revealed that the metal cofactor is a Fe2+ ion in Escherichia coli and many other bacterial PDFs. In this work, we found that PDFs from two iron-deficient bacteria, Borrelia burgdorferi and Lactobacillus plantarum, are stable and highly active under aerobic conditions. The native B. burgdoiferi PDF (BbPDF) was purified 1200-fold and metal analysis revealed that it contains similar to 1.1 Zn2+ ion/polypeptide but no iron. Our studies suggest that PDF utilizes different metal ions in different organisms. These data have important implications in designing PDF inhibitors and should help address some of the unresolved issues regarding PDF structure and catalytic function. (c) 2007 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据