PspE (phage-shock protein E) of Escherichia coli is a rhodanese.
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.
Adams
Hendrik
H
Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands. h.adams@bio.uu.nl
Teertstra
Wieke
W
Koster
Margot
M
Tommassen
Jan
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D007700:Kinetics; D008969:Molecular Sequence Data; D009876:Operon; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry / Q000502:physiology*
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; C069816:phage shock protein, Bacteria; D013884:Thiosulfate Sulfurtransferase