Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 468, Issue 2, Pages 217-225Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.09.023
Keywords
peptide deformylase; hydrolase; iron; zinc; metal specificity; catalysis
Categories
Funding
- NIAID NIH HHS [R01 AI062901, R01 AI040575-09, R01 AI062901-03, R01 AI040575, AI62901, AI40575] Funding Source: Medline
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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.
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