L-Selective amidase with extremely broad substrate specificity from Ochrobactrum anthropi NCIMB 40321

Authors :: Sonke, Theo
Ernste, Sandra
Tandler, Renate F.
Kaptein, Bernard
Peeters, Wilco P.H.
van Assema, Frisco B.J.
Wubbolts, Marcel G.
Schoemaker, Hans E.
Source :: Applied and Environmental Microbiology. Dec, 2005, Vol. 71 Issue 12, p7961, 13 p.
Publication Year :: 2005
Abstract: The purification, cloning and heterologous expression in Escherichia coli of the L-specific amidase from Ochrobactrum anthropi NCIMB 40321 wild-type cells are described. The results have shown that this amidase is responsible for the remarkably relaxed substrate specificity of this microorganism.

Subjects :: Cysteine proteinases -- Chemical properties
Serine -- Chemical properties
Escherichia coli -- Genetic aspects
Biological sciences

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