Determination of amino acid sequences of two subunits in sarcosine oxidase from Corynebacterium sp. U-96.
The primary structures of the C and D subunits of sarcosine oxidase from Corynebacterium 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 these two species, that is, four N-terminal residues were truncated in the C subunit, but six C-terminal residues were truncated in the D subunit. The D subunit contained three cysteine residues, but no disulfide bonds are in the subunit. Overall sequences of both subunit showed no homology with any other protein in the data base.
Mukouyama
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EB
Department of Biosciences, Faculty of Science, Kitasato University, Sagamihara, Kanagawa, Japan. mukoyama@jet.sci.kitasato-u.ac.jp
Tatemukai
S
S
Morioka
K
K
Matsuura
J
J
Suzuki
H
H
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D003352:Corynebacterium / Q000201:enzymology*; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry* / Q000302:isolation & purification; D050879:Sarcosine Oxidase; D017386:Sequence Homology, Amino Acid
D004220:Disulfides; D010089:Oxidoreductases, N-Demethylating; D050879:Sarcosine Oxidase