大肠杆菌的噬菌体休克蛋白E（PspE）是一种硫氰酸酶。
PspE (phage-shock protein E) of Escherichia coli is a rhodanese.
作者信息
Adams Hendrik, Teertstra Wieke, Koster Margot, Tommassen Jan
机构信息
Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
出版信息
FEBS Lett. 2002 May 8;518(1-3):173-6. doi: 10.1016/s0014-5793(02)02695-9.
The psp (phage-shock protein) operon of Escherichia coli is induced when the bacteria are infected by filamentous phage and under several other stress conditions. The physiological role of the individual Psp proteins is still not known. We demonstrate here that the last gene of the operon, pspE, encodes a thiosulfate:cyanide sulfurtransferase (EC 2.8.1.1; rhodanese). Kinetic analysis revealed that catalysis occurs via a double displacement mechanism as described for other rhodaneses. The K(m)s for SSO3(2-) and CN- were 4.6 and 27 mM, respectively.
大肠杆菌的噬菌体休克蛋白（psp）操纵子在细菌被丝状噬菌体感染以及在其他几种应激条件下会被诱导。各个Psp蛋白的生理作用仍不清楚。我们在此证明，该操纵子的最后一个基因pspE编码一种硫代硫酸盐：氰化物硫转移酶（EC 2.8.1.1；硫氰酸酶）。动力学分析表明，催化作用通过与其他硫氰酸酶相同的双置换机制发生。亚硫酸盐（SSO3(2-)）和氰化物（CN-）的米氏常数（K(m)）分别为4.6 mM和27 mM。
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