The cyanide hydratase enzyme of Fusarium lateritium also has nitrilase activity.
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.
Department of Chemical and Life Sciences, Waterford Institute of Technology, Cork Road, Waterford, Ireland.
Linda M
LM
Nolan
Padraigin A
PA
Harnedy
Peter
P
Turner
Audrey B
AB
Hearne
Catherine
C
O'Reilly
D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000378:metabolism*; D003486:Cyanides / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005670:Fusarium / Q000201:enzymology* / Q000235:genetics; D005800:Genes, Fungal; D006836:Hydro-Lyases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017386:Sequence Homology, Amino Acid
D003486:Cyanides; D000619:Aminohydrolases; C021867:nitrilase; D006836:Hydro-Lyases; C076848:cyanide hydratase