Cloning and sequence analysis of the aminopeptidase My gene from Mycoplasma salivarium.
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).
Shibata
K
K
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan.
Tsuchida
N
N
Watanabe
T
T
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D001426:Bacterial Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009174:Mycoplasma / Q000201:enzymology / Q000235:genetics*; D016415:Sequence Alignment; D017421:Sequence Analysis; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014364:Tryptophan / Q000235:genetics
D001426:Bacterial Proteins; D003062:Codon; D014364:Tryptophan; D000626:Aminopeptidases; C095710:aminopeptidase My, Mycoplasma salivarium