Determination of Amino Acid Sequences of Two Subunits in Sarcosine Oxidase from Corynebacterium sp. U-96
| Autor: | Kenji Morioka, Shoko Tatemukai, Junnosuke Matsuura, Etsuko B. Mukouyama, Haruo Suzuki |
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| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Sarcosine Sequence Homology Amino Acid Protein subunit Molecular Sequence Data Protein primary structure Oxidoreductases N-Demethylating Peptide Corynebacterium Sarcosine Oxidase Biology Biochemistry Amino acid chemistry.chemical_compound chemistry Chromatography Gel Electrophoresis Polyacrylamide Gel Amino Acid Sequence Disulfides Peptide sequence Sarcosine oxidase Cysteine |
| Zdroj: | Journal of Protein Chemistry. 18:747-752 |
| ISSN: | 1573-4943 0277-8033 |
| DOI: | 10.1023/a:1020625400518 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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