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J. Biochem, 1988, Vol. 104, No. 5 832-836
© 1988 Japanese Biochemical Society

research-article

Amino Acid Sequence of a Lysozyme (B-Enzyme) from Bacillus subtilis YT-251

Kaeko Kamei*, Saburo Hara*,2, Tokuji Ikenaka* and Sawao Murao**

*Department of Chemistry, Osaka University College of Science, Toyonaka Osaka 560
**Kumamoto Institute of Technology, Kumamoto Kumamoto 860

2 To whom all correspondence should be addressed

The amino acid sequence of a lysozyme, (B-enzyme), from Bacillus subtilis YT-25 was determined by conventional methods. B-Enzyme comprised 117 amino acid residues and had a heterogeneous sequence in the amino-terminal region. The amino acid sequence of B-enzyme was different from those of all other lysozymes the sequences of which are known. However, the partial amino acid sequence of Ser(74) to Ser(97) of B-enzyme was homologous with that of the active-site region of hen egg-white lysozyme (Ser(36) to Ser(60)), which includes one of the catalytic amino acids, Asp(52). It is interesting that B-enzyme has an amino acid sequence homologous with that of the gag protein p25 of the AIDS virus ARV-2.

1 This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan


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