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Cloning and sequence analysis of the aminopeptidase My gene from Mycoplasma salivarium
K Shibata1, N Tsuchida, T Watanabe
1Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan.
FEMS Microbiology Letters
|July 15, 1995
Abstract:
The complete nucleotide sequence of a major component of aminopeptidase My purified from Mycoplasma salivarium was determined. The protein gene encoded a protein consisting of 520 amino acids with a molecular mass of 58079 Da. The protein contained two tryptophan residues, one of which was encoded by UGA. A computer-aided homology search suggested that aminopeptidase My had properties similar to those of leucine aminopeptidase (EC 3.4.11.1).