Determination of the ionization state and catalytic function of Glu-133 in peptide deformylase by difference FTIR spectroscopy
Determination of the ionization state and catalytic function of Glu-133 in peptide deformylase by difference FTIR spectroscopy
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DOI：
10.1021/bi026137e
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发表时间：
2002-08-20
期刊：
影响因子：
2.9
通讯作者：
Pei, DH
中科院分区：
文献类型：
--
作者：
Deng, H;Callender, R;Pei, DH
肽脱甲酰基酶（PDF）催化水解去除真细菌和某些真核生物细胞器中新合成多肽的N-末端甲酰基。PDF是一类新型的酰胺水解酶，其利用Fe 2+离子来实现酰胺键的水解。亚铁离子由来自保守的HEXXH基序的两个组氨酸、半胱氨酸和水分子四面体配位。在这项工作中，保守的谷氨酸（Glu-133在大肠杆菌PDF）的功能进行了评估的差异傅立叶变换红外光谱分析的钴（II）取代的E。coli野生型和E133 D突变体PDF。在pH
Peptide deformylase (PDF) catalyzes the hydrolytic removal of the N-terminal formyl group from newly synthesized polypeptides in eubacteria and the organelles of certain eukaryotes. PDF is a novel class of amide hydrolase, which utilizes an Fe2+ ion to effect the hydrolysis of an amide bond. The ferrous ion is tetrahedrally coordinated by two histidines from a conserved HEXXH motif, a cysteine, and a water molecule. In this work, the function of the conserved glutamate (Glu-133 in Escherichia coli PDF) is evaluated by difference FTIR spectroscopic analysis of a Co(II)-substituted E. coli wild-type and E133D mutant PDF. At pH