Purification and characterization of a new enzyme, N-alkylglycine oxidase from Cladosporium sp. G-10.
A new enzyme, N-alkylglycine oxidase, was isolated from a soil mold, Cladosporium sp. G-10. This protein, which was purified to near homogeneity by ammonium sulfate precipitation followed by successive column chromatography on phenyl-Sepharose, DEAE-Sepharose and Sephadex G-200, was a single polypeptide with a molecular mass of 52,000. In the presence of O2 and H2O, this enzyme acted on some N-alkylglycine derivatives, such as N epsilon-carboxymethyllysine, N-carboxymethyl-6-aminocaproic acid, sarcosine and N-ethylglycine, and produced corresponding N-alkylamine, glyoxylic acid and H2O2. This enzyme had optimum activity at 30 degrees C, pH 8-10, and was most inhibited by ZnSO4, pCMB, iodoacetic acid, and SDS.
Gomi
K
K
Research and Development Division, Kikkoman Corporation, Chiba, Japan. 8553@mail.kikkoman.co.jp
Horiuchi
T
T
D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002963:Cladosporium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D008970:Molecular Weight; D012521:Sarcosine / Q000378:metabolism; D013696:Temperature