Cloning and expression of the creatinase gene from Flavobacterium sp. U-188 in Escherichia coli.
The gene coding for creatinase (creatine amidinohydrolase, EC 3.5.3.3) was isolated from Flavobacterium sp. U-188. The primary structure of creatinase deduced from the nucleotide sequence showed a protein (molecular weight, 42, 651) composed of 378 amino acids. The creatinase gene was over-expressed in Escherichia coli under the control of the lac promoter and the amount of this enzyme was over 20% of the soluble protein in the cell.
Koyama
Y
Y
Research and Development Division, Kikkoman Corporation, Chiba, Japan.
Kitao
S
S
Yamamoto-Otake
H
H
Suzuki
M
M
Nakano
E
E
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D005417:Flavobacterium / Q000201:enzymology* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D010957:Plasmids; D015183:Restriction Mapping; D014512:Ureohydrolases / Q000235:genetics*
D004269:DNA, Bacterial; D014512:Ureohydrolases; C019944:creatinase