Cloning and nucleotide sequence of amidase gene from Pseudomonas putida.
Amidases are a class of enzymes which convert amides to acids and have potential value in the development of commercial bioprocesses for the production of useful chemicals. A gene encoding an amidase in Pseudomonas putida 5B has been cloned, sequenced, and overexpressed in Escherichia coli. An additional open reading frame (P38K) encoding a putative protein of 38 kDa was found immediately upstream of the amidase gene. This work continues our characterization of a P. putida operon, which now appears to include P38K, amidase, and a stereo-specific nitrile hydratase. This characterization underlies continuing efforts in biocatalyst development.
Wu
S
S
DuPont Central Research and Development, Glasgow Site, Newark, DE 19714-6101, USA.
Fallon
R D
RD
Payne
M S
MS
D000581:Amidohydrolases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009876:Operon; D016958:Pseudomonas putida / Q000201:enzymology* / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D012045:Regulatory Sequences, Nucleic Acid; D015183:Restriction Mapping
D011994:Recombinant Proteins; D000581:Amidohydrolases; C019665:amidase