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J. Biochem, 1986, Vol. 99, No. 5 1537-1539
© 1986 Japanese Biochemical Society

other

Isolation and Amino Acid Sequence of a Peptide Containing an Epoxide-Reactive Residue from the Thermolysin-Digest of Scytalidium lignicolum Acid Protease B1

Daisuke TSURU*,2, Shinya SHIMADA*, Shinsaku MARUTA*, Tadashi YOSHIMOTO*, Kohei ODA**, Sawao MURAO**, Toshiyuki MIYATA*** and Sadaaki IWANAGA***

*Faculty of Pharmaceutical Sciences, Nagasaki University Nagasaki, Nagasaki 852
**Department of Agricultural Chemistry, University of Osaka Prefecture Sakai, Osaka 591
***Department of Biology Faculty of Sciences, Kyushu University Fukuoka, Fukuoka 821

2 To whom reprint request should be addressed at Faculty of Pharmaceutical Sciences, Nagasaki University, Bunkyo-machi 1–14, Nagasaki 852.

Scytalidium lignicolum acid protease B, a pepstatin-insensitive acid protease, was modified by 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) with the concomitant loss of its enzyme activity, and an EPNP-labeled peptide was isolated from the thermolysin-digest of the modified enzyme by HPLC. The amino acid sequence of the peptide was determined to be Ile-Leu-Glu-Thr-Gly, which corresponds to the sequence of residue Nos. 51–55 of the enzyme. The results of treatment of the labeled peptide with hydroxylamine suggested that the EPNP moiety is ester-linked to Glu53 of the enzyme. The amino acid sequence around Glu53 of the acid protease B showed high homology with those around the active site Asp residues of calf chymosin and porcine pepsin. These results show that it is highly possible that Glu53 of the acid protease B is one of the amino acid residues involved in its catalytic activity.

1 This work was supported in part by a grant from the Ministry of Education, Science and Culture of Japan.


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