The cyanide hydratase enzyme of Fusarium lateritium also has nitrilase activity

Linda M. Nolan, Padraigin A. Harnedy, Peter Turner, Audrey B. Hearne, Catherine O’reilly

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)

Abstract

The filamentous fungus Fusarium lateritium produces cyanide hydratase when grown in the presence of cyanide. The cyanide hydratase protein produced at a high level in Escherichia coli shows a low but significant nitrilase activity with acetonitrile, propionitrile and benzonitrile. The nitrilase activity is sufficient for growth of the recombinant strain on acetonitrile, propionitrile or benzonitrile as the sole source of nitrogen. The recombinant enzyme shows highest nitrilase activity with benzonitrile. Site-directed mutagenesis of the F. lateritium cyanide hydratase gene indicates that mutations leading to a loss of cyanide hydratase activity also lead to a loss of nitrilase activity. This suggests that the active site for cyanide hydratase and nitrilase activity in the protein is the same. This is the first evidence of cyanide hydratase having nitrilase activity.

Original languageEnglish
Pages (from-to)161-165
Number of pages5
JournalFEMS Microbiology Letters
Volume221
Issue number2
DOIs
Publication statusPublished - 25 Apr 2003

Keywords

  • Cyanide hydratase
  • Nitrilase
  • Nitrile
  • Site-directed mutagenesis

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