PMID: 2111259Mar 15, 1990Paper

The role of histidine residues in the alpha toxin of Clostridium perfringens

FEMS Microbiology Letters
R W Titball, T Rubidge

Abstract

The alpha-toxin (phospholipase C) of Clostridium perfringens has been reported to contain catalytically essential zinc ions. We report here that histidine residues are essential for the co-ordination of these ion(s). Incubation of alpha toxin with diethylpyrocarbonate, a histidine modifying reagent, did not result in the loss of phospholipase C activity unless the protein was first incubated with EDTA, suggesting that zinc ions normally protect the susceptible histidine residues. When the amino acid sequences of three phospholipase C's were aligned, essential zinc binding histidine residues in the non-toxic B. cereus phospholipase C were found in similar positions in the toxic C. perfringens enzyme and the weakly toxic C. bifermentans phospholipase C.

References

Mar 1, 1979·Reviews of Infectious Diseases·L D Smith
Jun 24, 1975·Biochimica Et Biophysica Acta·C Little, A B Otnåss
Jun 1, 1986·Applied and Environmental Microbiology·O P Shukla
Jan 1, 1988·The Journal of Clinical Investigation·A C RybickiR S Schwartz
Jun 1, 1984·Archives of Biochemistry and Biophysics·E L Krug, C Kent

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Citations

Sep 29, 2000·Microbes and Infection·M Jepson, R Titball
Jan 1, 1996·Microbiology and Immunology·M Nagahama, J Sakurai
Jun 28, 2011·Biochimica Et Biophysica Acta·Patricia UrbinaMarc F Lensink
Aug 5, 2006·Anaerobe·R W TitballA K Basak
Sep 10, 2005·Microbiology·Richard W Titball
Feb 1, 1989·FEMS Microbiology Letters·P Röger, F Lingens
Aug 1, 1996·Applied and Environmental Microbiology·S D SuttonJ R Vestal

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