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 Previous Article

Journal of Bacteriology, November 2007, p. 7942-7944, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00922-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for Maturation of Escherichia coli Hydrogenase{triangledown}

Jie Wei Zhang, Michael R. Leach, and Deborah B. Zamble*

Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6

Received 12 June 2007/ Accepted 17 August 2007

Escherichia coli SlyD, which is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, exhibits several activities including that of a peptidyl-prolyl isomerase (PPIase). Mutations that result in deficient PPIase activity do not produce corresponding decreases in the other activities of SlyD in vitro or in hydrogenase production levels in vivo.

* Corresponding author. Mailing address: Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6. Phone and fax: (416) 978-3568. E-mail: dzamble{at}chem.utoronto.ca

{triangledown} Published ahead of print on 24 August 2007.

Journal of Bacteriology, November 2007, p. 7942-7944, Vol. 189, No. 21
0021-9193/07/$08.00+0     doi:10.1128/JB.00922-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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