Open AccessCloning and sequence analysis of the aminopeptidase My gene from Mycoplasma salivarium
Author(s) -
Shibata Kenichiro,
Tsuchida Nobuo,
Watanabe Tsuguo
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07691.x
Subject(s) - aminopeptidase , nucleic acid sequence , gene , homology (biology) , biology , peptide sequence , amino acid , leucine , cloning (programming) , sequence analysis , biochemistry , genetics , microbiology and biotechnology , computer science , programming language
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).