Determination of amino acid sequences of two subunits in sarcosine oxidasefrom Corynebacterium sp U-96

The primary structures of the C and D subunits of sarcosine oxidase from Co rynebacterium sp. U-96 were determined by sequencing the peptide fragments derived from their enzymatic digestions. The C and D subunits were shown to be composed of 199 and 92 residues, respectively. Each amino acid sequence showed a high homology with the sequence of the corresponding subunit from Corynebacterium sp. P-1. However, there were some differences between thes e two species, that is, four N-terminal residues were truncated in the C su bunit, but six C-terminal residues were truncated in the D subunit. The D s ubunit contained three cysteine residues, but no disulfide bonds are in the subunit. Overall sequences of both subunit showed no homology with any oth er protein in the data base.