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锌是伯氏疏螺旋体肽脱甲酰基酶的金属辅因子。

Zinc is the metal cofactor of Borrelia burgdorferi peptide deformylase.

作者信息

Nguyen Kiet T, Wu Jen-Chieh, Boylan Julie A, Gherardini Frank C, Pei Dehua

机构信息

Department of Chemistry and Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.

出版信息

Arch Biochem Biophys. 2007 Dec 15;468(2):217-25. doi: 10.1016/j.abb.2007.09.023. Epub 2007 Oct 5.

DOI:10.1016/j.abb.2007.09.023
PMID:17977509
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2151311/
Abstract

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. burgdorferi PDF (BbPDF) was purified 1200-fold and metal analysis revealed that it contains approximately 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.

摘要

肽脱甲酰基酶（PDF，E.C. 3.5.1.88）催化从新生核糖体合成的多肽中去除N端甲酰基。PDF含有一个催化必需的二价金属离子，该离子由三个蛋白质配体（组氨酸、组氨酸和半胱氨酸）和一个水分子以四面体方式配位。先前的研究表明，金属辅因子在大肠杆菌和许多其他细菌的PDF中是Fe2+离子。在这项工作中，我们发现来自两种缺铁细菌——伯氏疏螺旋体和植物乳杆菌的PDF在有氧条件下是稳定且高度活跃的。天然的伯氏疏螺旋体PDF（BbPDF）被纯化了1200倍，金属分析表明它每多肽含有约1.1个Zn2+离子但不含铁。我们的研究表明，PDF在不同生物体中利用不同的金属离子。这些数据对设计PDF抑制剂具有重要意义，并应有助于解决一些关于PDF结构和催化功能的未解决问题。

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