DB code: D00235

RLCP classification 1.13.10900.463 : Hydrolysis
CATH domain 3.10.170.10 : Elastase; domain 1 Catalytic domain
1.10.390.10 : Neutral Protease; domain 2 Catalytic domain
E.C. 3.4.24.28
CSA
M-CSA
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P05806 Bacillolysin
EC 3.4.24.28
Neutral protease
M04.001 (Metallo)
PF07504 (FTP)
PF03413 (PepSY)
PF01447 (Peptidase_M4)
PF02868 (Peptidase_M4_C)
[Graphical View]

KEGG enzyme name
bacillolysin
Bacillus metalloendopeptidase
Bacillus subtilis neutral proteinase
anilozyme P 10
Bacillus metalloproteinase
Bacillus neutral proteinase
megateriopeptidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P05806 NPRE_BACCE Similar, but not identical, to that of thermolysin. Secreted. Binds 4 calcium ions per subunit. Binds 1 zinc ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00017 C00012 C00001 C00017 C00012
E.C.
Compound Zinc Protein Peptide H2O Protein Peptide
Type heavy metal peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 29105
15377
PubChem 32051
22247451
962
1espA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound
1npcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound
1espA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound
1npcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1esp, 1npc & Swiss-prot;P05806

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1espA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 113; HIS 143;HIS 147(Zinc binding) ALA 114 mutant E144S
1npcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 113;GLU 144 HIS 143;HIS 147(Zinc binding) ALA 114
1espA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 158;HIS 232 GLU 167(Zinc binding)
1npcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 158;HIS 232 GLU 167(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 88172498
PubMed ID 3127592
Journal J Mol Biol
Year 1988
Volume 199
Pages 525-37
Authors Pauptit RA, Karlsson R, Picot D, Jenkins JA, Niklaus-Reimer AS, Jansonius JN
Title Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin.
Related PDB
Related UniProtKB P05806
[2]
Resource
Comments
Medline ID
PubMed ID 2124807
Journal Biochem J
Year 1990
Volume 272
Pages 93-7
Authors van den Burg B, Eijsink VG, Stulp BK, Venema G
Title Identification of autodigestion target sites in Bacillus subtilis neutral proteinase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1899021
Journal Biochemistry
Year 1991
Volume 30
Pages 97-106
Authors Toma S, Campagnoli S, Margarit I, Gianna R, Grandi G, Bolognesi M, De Filippis V, Fontana A
Title Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1817257
Journal Protein Eng
Year 1991
Volume 4
Pages 941-5
Authors Vriend G, Berendsen HJ, van der Zee JR, van den Burg B, Venema G, Eijsink VG
Title Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 92339470
PubMed ID 1633827
Journal Eur J Biochem
Year 1992
Volume 207
Pages 781-91
Authors Stark W, Pauptit RA, Wilson KS, Jansonius JN
Title The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
Related PDB 1npc
Related UniProtKB P05806
[6]
Resource
Comments
Medline ID
PubMed ID 1518790
Journal Protein Eng
Year 1992
Volume 5
Pages 421-6
Authors Eijsink VG, Dijkstra BW, Vriend G, van der Zee JR, Veltman OR, van der Vinne B, van den Burg B, Kempe S, Venema G
Title The effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1594570
Journal Protein Eng
Year 1992
Volume 5
Pages 157-63
Authors Eijsink VG, Vriend G, van den Burg B, van der Zee JR, Veltman OR, Stulp BK, Venema G
Title Introduction of a stabilizing 10 residue beta-hairpin in Bacillus subtilis neutral protease.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 1594571
Journal Protein Eng
Year 1992
Volume 5
Pages 165-70
Authors Eijsink VG, Vriend G, van den Burg B, van der Zee JR, Venema G
Title Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8415578
Journal Protein Eng
Year 1993
Volume 6
Pages 521-7
Authors van den Burg B, Dijkstra BW, van der Vinne B, Stulp BK, Eijsink VG, Venema G
Title Introduction of disulfide bonds into Bacillus subtilis neutral protease.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8143751
Journal Eur J Biochem
Year 1994
Volume 220
Pages 981-5
Authors Van den Burg B, Dijkstra BW, Vriend G, Van der Vinne B, Venema G, Eijsink VG
Title Protein stabilization by hydrophobic interactions at the surface.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8177891
Journal Protein Eng
Year 1994
Volume 7
Pages 425-30
Authors Hardy F, Vriend G, van der Vinne B, Frigerio F, Grandi G, Venema G, Eijsink VG
Title The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.
Medline ID
PubMed ID
Journal Acta Crystallogr D Biol Crystallogr
Year 1996
Volume 52
Pages 543-50
Authors Lister SA, Wetmore DR, Roche RS, Codding PW
Title E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8-A resolution.
Related PDB 1esp
Related UniProtKB P05806
[13]
Resource
Comments
Medline ID
PubMed ID 9761816
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 45-57
Authors Carfi A, Duee E, Paul-Soto R, Galleni M, Frere JM, Dideberg O
Title X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9569607
Journal Biotechnol Appl Biochem
Year 1998
Volume 27
Pages 125-32
Authors Van den Burg B, Eijsink VG, Vriend G, Veltman OR, Venema G
Title Rendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 10611287
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 14765-70
Authors Rudner DZ, Fawcett P, Losick R
Title A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors.
Related PDB
Related UniProtKB

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.

Created Updated
2005-04-13 2009-02-26