EzCatDB: D00235
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00235
RLCP classification1.13.10900.463 : Hydrolysis
CATH domainDomain 13.10.170.10 : Elastase; domain 1Catalytic domain
Domain 21.10.390.10 : Neutral Protease; domain 2Catalytic domain
E.C.3.4.24.28

CATH domainRelated DB codes (homologues)
1.10.390.10 : Neutral Protease; domain 2D00233,D00234,D00480
3.10.170.10 : Elastase; domain 1D00233,D00234,D00480

Enzyme Name
UniProtKBKEGG

P05806
Protein nameBacillolysinbacillolysin
Bacillus metalloendopeptidase
Bacillus subtilis neutral proteinase
anilozyme P 10
Bacillus metalloproteinase
Bacillus neutral proteinase
megateriopeptidase
SynonymsEC 3.4.24.28
Neutral protease
MEROPSM04.001 (Metallo)
PfamPF07504 (FTP)
PF03413 (PepSY)
PF01447 (Peptidase_M4)
PF02868 (Peptidase_M4_C)
[Graphical view]


UniProtKB:Accession NumberP05806
Entry nameNPRE_BACCE
ActivitySimilar, but not identical, to that of thermolysin.
Subunit
Subcellular locationSecreted.
CofactorBinds 4 calcium ions per subunit.,Binds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00017C00012C00001C00017C00012
CompoundZincProteinPeptideH2OProteinPeptide
Typeheavy metalpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI29105


15377


PubChem32051


962
22247451


              
1espA01Bound:_ZNUnboundUnbound UnboundUnbound
1npcA01Bound:_ZNUnboundUnbound UnboundUnbound
1espA02Bound:_ZNUnboundUnbound UnboundUnbound
1npcA02Bound:_ZNUnboundUnbound UnboundUnbound

Active-site residues
resource
PDB;1esp, 1npc & Swiss-prot;P05806
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
1espA01ASN 113;       
HIS 143;HIS 147(Zinc binding)
ALA 114
mutant E144S
1npcA01ASN 113;GLU 144
HIS 143;HIS 147(Zinc binding)
ALA 114
 
1espA02TYR 158;HIS 232
GLU 167(Zinc binding)
 
 
1npcA02TYR 158;HIS 232
GLU 167(Zinc binding)
 
 


references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID88172498
PubMed ID3127592
JournalJ Mol Biol
Year1988
Volume199
Pages525-37
AuthorsPauptit RA, Karlsson R, Picot D, Jenkins JA, Niklaus-Reimer AS, Jansonius JN
TitleCrystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin.
Related UniProtKBP05806
[2]
PubMed ID2124807
JournalBiochem J
Year1990
Volume272
Pages93-7
Authorsvan den Burg B, Eijsink VG, Stulp BK, Venema G
TitleIdentification of autodigestion target sites in Bacillus subtilis neutral proteinase.
[3]
PubMed ID1899021
JournalBiochemistry
Year1991
Volume30
Pages97-106
AuthorsToma S, Campagnoli S, Margarit I, Gianna R, Grandi G, Bolognesi M, De Filippis V, Fontana A
TitleGrafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease.
[4]
PubMed ID1817257
JournalProtein Eng
Year1991
Volume4
Pages941-5
AuthorsVriend G, Berendsen HJ, van der Zee JR, van den Burg B, Venema G, Eijsink VG
TitleStabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID92339470
PubMed ID1633827
JournalEur J Biochem
Year1992
Volume207
Pages781-91
AuthorsStark W, Pauptit RA, Wilson KS, Jansonius JN
TitleThe structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
Related PDB1npc
Related UniProtKBP05806
[6]
PubMed ID1518790
JournalProtein Eng
Year1992
Volume5
Pages421-6
AuthorsEijsink VG, Dijkstra BW, Vriend G, van der Zee JR, Veltman OR, van der Vinne B, van den Burg B, Kempe S, Venema G
TitleThe effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease.
[7]
PubMed ID1594570
JournalProtein Eng
Year1992
Volume5
Pages157-63
AuthorsEijsink VG, Vriend G, van den Burg B, van der Zee JR, Veltman OR, Stulp BK, Venema G
TitleIntroduction of a stabilizing 10 residue beta-hairpin in Bacillus subtilis neutral protease.
[8]
PubMed ID1594571
JournalProtein Eng
Year1992
Volume5
Pages165-70
AuthorsEijsink VG, Vriend G, van den Burg B, van der Zee JR, Venema G
TitleIncreasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices.
[9]
PubMed ID8415578
JournalProtein Eng
Year1993
Volume6
Pages521-7
Authorsvan den Burg B, Dijkstra BW, van der Vinne B, Stulp BK, Eijsink VG, Venema G
TitleIntroduction of disulfide bonds into Bacillus subtilis neutral protease.
[10]
PubMed ID8143751
JournalEur J Biochem
Year1994
Volume220
Pages981-5
AuthorsVan den Burg B, Dijkstra BW, Vriend G, Van der Vinne B, Venema G, Eijsink VG
TitleProtein stabilization by hydrophobic interactions at the surface.
[11]
PubMed ID8177891
JournalProtein Eng
Year1994
Volume7
Pages425-30
AuthorsHardy F, Vriend G, van der Vinne B, Frigerio F, Grandi G, Venema G, Eijsink VG
TitleThe effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages543-50
AuthorsLister SA, Wetmore DR, Roche RS, Codding PW
TitleE144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8-A resolution.
Related PDB1esp
Related UniProtKBP05806
[13]
PubMed ID9761816
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages45-57
AuthorsCarfi A, Duee E, Paul-Soto R, Galleni M, Frere JM, Dideberg O
TitleX-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
[14]
PubMed ID9569607
JournalBiotechnol Appl Biochem
Year1998
Volume27
Pages125-32
AuthorsVan den Burg B, Eijsink VG, Vriend G, Veltman OR, Venema G
TitleRendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission.
[15]
PubMed ID10611287
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages14765-70
AuthorsRudner DZ, Fawcett P, Losick R
TitleA family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors.

comments
This enzyme belongs to peptidase family-M4 (Thermolysin family).
Although this enzyme binds four calcium ions, they are not involved in catalysis.
As the active site is the same as the thermolysin (D00234 in EzCatDB), the catalytic mechanism must be the same.

createdupdated
2005-04-132009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.