PspE (phage-shock protein E) of Escherichia coli is a rhodanese.

Abstract

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.

• Authors: Hendrik Adams, Wieke Teertstra, Margot Koster, Jan Tommassen
• Journal: FEBS letters (FEBS Lett) Vol. 518 Issue 1-3 Pg. 173-6 (May 08 2002) ISSN: 0014-5793 [Print] England
• PMID: 11997041 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Heat-Shock Proteins
• phage shock protein, Bacteria
• Thiosulfate Sulfurtransferase

Topics

• Amino Acid Sequence
• Bacterial Proteins (chemistry, physiology)
• Escherichia coli (enzymology)
• Heat-Shock Proteins (chemistry, physiology)
• Kinetics
• Molecular Sequence Data
• Operon
• Protein Structure, Secondary
• Sequence Homology, Amino Acid
• Thiosulfate Sulfurtransferase (chemistry, physiology)