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Reference on EC 3.4.21.B48 - kumamolysin

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Dunn, B.M.; Oda, K.
Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases
Acta Biochim. Pol.
50
81-102
2003
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Oda, K.; Ogasawara, S.; Oyama, H.; Dunn, B.M.
Subsite preferences of pepstatin-insensitive carboxyl proteinases from prokaryotes: kumamolysin, a thermostable pepstatin-insensitive carboxyl proteinase
J. Biochem.
128
499-507
2000
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Oyama, H.; Hamada, T.; Ogasawara, S.; Uchida, K.; Murao, S.; Beyer, B.B.; Dunn, B.M.; Oda, K.
A CLN2-related and thermostable serine-carboxyl proteinase, kumamolysin: cloning, expression, and identification of catalytic serine residue
J. Biochem.
131
757-765
2002
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Murao, S.; Ohkuni, K.; Nagao, M.; Hirayama, K.; Fukuhara, K.; Oda, K.; Oyama, H.; Shin, T.
Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32
J. Biol. Chem.
268
349-355
1993
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Wlodawer, A.; Li, M.; Gustchina, A.; Tsuruoka, N.; Ashida, M.; Minakata, H.; Oyama, H.; Oda, K.; Nishino, T.; Nakayama, T.
Crystallographic and biochemical investigations of kumamolisin-AS a serine-carboxyl peptidase with collagenase activity
J. Biol. Chem.
279
21500-21510
2004
Alicyclobacillus sendaiensis, Alicyclobacillus sendaiensis NTAP-2
Manually annotated by BRENDA team
Comellas-Bigler, M.; Fuentes-Prior, P.; Maskos, K.; Huber, R.; Oyama, H.; Uchida, K.; Dunn, B.M.; Oda, K.; Bode, W.
The 1.4 A crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase
Structure
10
865-876
2002
Bacillus sp. (in: Bacteria) (Q8RR56), Bacillus sp. (in: Bacteria) MN-32 (Q8RR56)
Manually annotated by BRENDA team
Comellas-Bigler, M.; Maskos, K.; Huber, R.; Oyama, H.; Oda, K.; Bode, W.
1.2 A Crystal structure of the serine carboxyl proteinase pro-kumamolisin: structure of an intact pro-subtilase
Structure
12
1313-1323
2004
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Fujimoto, Y.; Ikeuchi, H.; Tada, T.; Oyama, H.; Oda, K.; Kunugi, S.
Synergetic effects of pressure and chemical denaturant on protein unfolding: stability of a serine-type carboxyl protease, kumamolisin
Biochim. Biophys. Acta
1764
364-371
2006
Bacillus novosp., Bacillus novosp. MN-32
Manually annotated by BRENDA team
Okubo, A.; Li, M.; Ashida, M.; Oyama, H.; Gustchina, A.; Oda, K.; Dunn, B.M.; Wlodawer, A.; Nakayama, T.
Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site
FEBS J.
273
2563-2576
2006
Alicyclobacillus sendaiensis, Alicyclobacillus sendaiensis NTAP-1
Manually annotated by BRENDA team
Oda, K.
Kumamolisin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2nd Ed.
1889-1891
2004
Bacillus novosp., Bacillus novosp. MN-32, Weizmannia coagulans, Weizmannia coagulans J-4
-
Manually annotated by BRENDA team
Catara, G.; Fiume, I.; Iuliano, F.; Maria, G.; Ruggiero, G.; Palmieri, G.; Capasso, A.; Rossi, M.
A new kumamolisin-like protease from Alicyclobacillus acidocaldarius: an enzyme active under extreme acidic conditions
Biocatal. Biotransform.
24
358-370
2006
Alicyclobacillus acidocaldarius
-
Manually annotated by BRENDA team
Xu, Q.; Li, L.; Guo, H.
Understanding the mechanism of deacylation reaction catalyzed by the serine carboxyl peptidase kumamolisin-As: insights from QM/MM free energy simulations
J. Phys. Chem. B
114
10594-10600
2010
Homo sapiens
Manually annotated by BRENDA team
Yao, J.; Wlodawer, A.; Guo, H.
Understanding the autocatalytic process of pro-kumamolisin activation from molecular dynamics and quantum mechanical/molecular mechanical (QM/MM) free-energy simulations
Chem. Eur. J.
19
10849-10852
2013
Bacillus sp. (in: Bacteria) (Q8RR56), Bacillus sp. (in: Bacteria) MN-32 (Q8RR56)
Manually annotated by BRENDA team