Reaction: The enzyme preferentially hydrolyses peptides having an Ala or Pro residue at P2 position and prefers such charged amino acid residues as Glu or Arg at the P2' position. In the oxidized insulin B chain, kumamolysin preferentially cleaves between Leu15 and Tyr16
Other name(s): KSCP; kumamolisin
Comments: This bacterial pepstatin-insensitive carboxyl proteinase has been isolated and characterized from Bacillus sp. MN-32 and from several Burkholderia spp. Kumamolysin from Bacillus sp. MN-32 exhibits a Ser278/Glu78/Asp82 catalytic triad. The enzyme is a type example of peptidase family S53 in the MEROPS Peptidas Database.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Murao, S., Ohkuni, K., Nagao, M., Hirayama, K., Fukuhara, K., Oda, K., Oyama, H. and Shin, T. Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32. J. Biol. Chem. 268 (1993) 349-355. [PMID: 8416942]
2. Oda, K., Ogasawara, S., Oyama, H. and Dunn, B.M. Subsite preferences of pepstatin-insensitive carboxyl proteinases from prokaryotes: kumamolysin, a thermostable pepstatin-insensitive carboxyl proteinase. J. Biochem. 128 (2000) 499-507. [PMID: 10965051]
3. Oyama, H., Hamada, T., Ogasawara, S., Uchida, K., Murao, S., Beyer, B.B., Dunn, B.M. and Oda, K. A CLN2-related and thermostable serine-carboxyl proteinase, kumamolysin: cloning, expression, and identification of catalytic serine residue. J. Biochem. 131 (2002) 757-765. [PMID: 11983085]
4. Comellas-Bigler, M., Fuentes-Prior, P., Maskos, K., Huber, R., Oyama, H., Uchida, K., Dunn, B.M., Oda, K. and Bode, W. The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase. Structure 10 (2002) 865-876. [PMID: 12057200]
5. Wlodawer, A., Li, M., Gustchina, A., Tsuruoka, N., Ashida, M., Minakata, H., Oyama, H., Oda, K., Nishino, T. and Nakayama, T. Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity. J. Biol. Chem. 279 (2004) 21500-21510. [PMID: 15014068]