Meinnel T, Blanquet S
Laboratoire de Biochimie, Unité de Recherche Associée, no. 240 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.
J Bacteriol. 1993 Dec;175(23):7737-40. doi: 10.1128/jb.175.23.7737-7740.1993.
Overexpression of the fms gene, the first translation unit of a dicistronic operon that also encodes methionyl-tRNA(fMet) formyltransferase in Escherichia coli, sustains the overproduction of peptide deformylase activity in crude extracts. This suggests that the fms gene encodes the peptide deformylase. Moreover, the fms gene product has a motif characteristic of metalloproteases, an activity compatible with deformylase. The corresponding protein could be purified to homogeneity. However, its enzymatic activity could not be retained during the purification procedure. As could be expected from the occurrence in its amino acid sequence of a zinc-binding motif characteristic of metallopeptidases, the purified fms product displayed one tightly bound zinc atom.
fms基因是大肠杆菌中一个双顺反子操纵子的第一个翻译单元，该操纵子还编码甲硫氨酰 - tRNA（fMet）甲酰基转移酶，其过表达能维持粗提物中肽脱甲酰酶活性的过量产生。这表明fms基因编码肽脱甲酰酶。此外，fms基因产物具有金属蛋白酶的特征基序，这是一种与脱甲酰酶兼容的活性。相应的蛋白质可以纯化至同质。然而，在纯化过程中其酶活性无法保留。正如从其氨基酸序列中出现金属肽酶特有的锌结合基序所预期的那样，纯化的fms产物显示有一个紧密结合的锌原子。
