KEGG   ENZYME: 3.4.24.28Help
Entry
EC 3.4.24.28                Enzyme                                 

Name
bacillolysin;
Bacillus metalloendopeptidase;
Bacillus subtilis neutral proteinase;
anilozyme P 10;
Bacillus metalloproteinase;
Bacillus neutral proteinase;
megateriopeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Similar, but not identical, to that of thermolysin
Comment
Variants of this enzyme have been found in species of Bacillus including B. subtilis [1,6], B. amyloliquefaciens [5], B. megaterium (megateriopeptidase, [2]), B. mesentericus [10], B. cereus [3,8,9] and B. stearothermophilus [7]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4
History
EC 3.4.24.28 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.28
Orthology
K01400  bacillolysin
Genes
SAGA: M5M_09630
WOC: BA177_08085
MFU: LILAB_34165
MSD: MYSTI_00607 MYSTI_01772
CCX: COCOR_00799(npr) COCOR_01296(nprM) COCOR_06712(nprM1)
AGE: AA314_00679 AA314_02845 AA314_04696 AA314_05743 AA314_08228
MBD: MEBOL_000603 MEBOL_003403 MEBOL_003411 MEBOL_004624
CFUS: CYFUS_000044 CYFUS_000703 CYFUS_002522 CYFUS_003038 CYFUS_004891 CYFUS_009605
VIN: AKJ08_0973
CCRO: CMC5_042380
BSU: BSU14700(nprE)
BSR: I33_1652
BSL: A7A1_0557
BSH: BSU6051_14700(nprE)
BSUT: BSUB_01599(nprE)
BSUL: BSUA_01599(nprE)
BSUS: Q433_08425
BSS: BSUW23_07570(nprE)
BST: GYO_1812
BSO: BSNT_07973(nprE)
BSQ: B657_14700(nprE)
BSX: C663_1514(nprE)
BAY: RBAM_014550(nprE)
BAQ: BACAU_1430(npr)
BYA: BANAU_1393(npr)
BAMP: B938_07575
BAML: BAM5036_1392(nprE)
BAMA: RBAU_1436(nprE)
BAMN: BASU_1416(nprE)
BAMB: BAPNAU_2298(npr)
BAMT: AJ82_08345
BAMY: V529_14130(nprE)
BMP: NG74_01512(npr)
BAO: BAMF_1546(nprE)
BAZ: BAMTA208_09795(nprE)
BQL: LL3_01578(nprE)
BXH: BAXH7_01996(npr)
BQY: MUS_1567(nprE)
BAMI: KSO_012080
BAMC: U471_14890
BAMF: U722_07735
BATR: TD68_04605
BAN: BA_0599
BAR: GBAA_0599
BAT: BAS0567
BAI: BAA_0683
BANT: A16_06580
BANR: A16R_06670
BANS: BAPAT_0578
BANV: DJ46_5058(npr)
BCE: BC0602
BCA: BCE_0667
BCZ: BCE33L0511(npr) pE33L466_0375(npr)
BCQ: BCQ_0665(npr) BCQ_PI139
BAL: BACI_c06090(npr1)
BCER: BCK_05145
BTK: BT9727_0509(npr)
BTL: BALH_0539(nprE) BALH_2915(npr)
BTT: HD73_0673
BTHI: BTK_03405
BTM: MC28_5326(npr)
BTG: BTB_c06140(npr1)
BTI: BTG_18155
BTW: BF38_1848(npr)
BWW: bwei_5002(npr)
BMYO: BG05_5325(npr)
BMYC: DJ92_2128(nprB) DJ92_3204(npr) DJ92_5598(nprM)
BMQ: BMQ_2326(nprM)
BMD: BMD_2285(nprM)
BMEG: BG04_4696(nprM)
BJS: MY9_1610
BACP: SB24_02420
BACB: OY17_10370
BACY: QF06_06375
BACL: BS34A_16300(nprE)
BALM: BsLM_1565
GEA: GARCT_02867(nprT) GARCT_03224(nprS)
ANM: GFC28_3256(npr)
ANL: GFC29_2178(npr)
HHD: HBHAL_4199(npr2) HBHAL_4829(npr4)
VPN: A21D_00581(nprE)
ESI: Exig_2940
EAN: Eab7_2752
BBE: BBR47_13290(npr)
PPM: PPSC2_20195(npr)
PPO: PPM_4046(npr)
PPQ: PPSQR21_040810(lasB)
PPOY: RE92_17000
PLV: ERIC2_c17790(npr1) ERIC2_c23330(npr2) ERIC2_c25850(npr3)
PRI: PRIO_3659(npr)
CAC: CA_C2290(nprE) CA_C2517(nrpE)
CAE: SMB_G2324 SMB_G2552(nprE)
CBO: CBO1446
CBA: CLB_1471(npr-6)
CBH: CLC_1483(npr-6)
CBY: CLM_1609
CBL: CLK_0927
CBB: CLD_3104
CBI: CLJ_B1548(npr_5)
CBF: CLI_1530
CBM: CBF_1509
CLD: CLSPO_c14680(npr1) CLSPO_c14690(nprM1) CLSPO_c14720(nprM4) CLSPO_c14730(nprM2)
HSC: HVS_05615(nprM)
ABAC: LuPra_01551(npr_2)
FLM: MY04_3789
GFL: GRFL_1314
FIN: KQS_02660
CHZ: CHSO_4198
FBU: UJ101_00424(nprB)
 » show all
Taxonomy
Reference
1  [PMID:4967801]
  Authors
Morihara K, Tsuzuki H, Oka T.
  Title
Comparison of the specificities of various neutral proteinases from microorganisms.
  Journal
Arch Biochem Biophys 123:572-88 (1968)
DOI:10.1016/0003-9861(68)90179-3
Reference
2  [PMID:4980359]
  Authors
Millet J, Acher R.
  Title
[Specificity of megateriopeptidase: an amino-endopeptidase with hydrophobic characteristics]
  Journal
Eur J Biochem 9:456-62 (1969)
DOI:10.1111/j.1432-1033.1969.tb00631.x
Reference
3  [PMID:5002444]
  Authors
Feder J, Keay L, Garrett LR, Cirulis N, Moseley MH, Wildi BS.
  Title
Bacillus cereus neutral protease.
  Journal
Biochim Biophys Acta 251:74-8 (1971)
DOI:10.1016/0005-2795(71)90061-4
Reference
4  [PMID:2276]
  Authors
Holmquist B, Vallee BL.
  Title
Esterase activity of zinc neutral proteases.
  Journal
Biochemistry 15:101-7 (1976)
Reference
5  [PMID:6090391]
  Authors
Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D.
  Title
Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein.
  Journal
J Bacteriol 159:811-9 (1984)
  Sequence
[bao:BAMF_1546]
Reference
6  [PMID:6090407]
  Authors
Yang MY, Ferrari E, Henner DJ.
  Title
Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation.
  Journal
J Bacteriol 160:15-21 (1984)
  Sequence
[bsu:BSU14700]
Reference
7  [PMID:2993245]
  Authors
Takagi M, Imanaka T, Aiba S.
  Title
Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus.
  Journal
J Bacteriol 163:824-31 (1985)
  Sequence
Reference
8  [PMID:3092843]
  Authors
Sidler W, Niederer E, Suter F, Zuber H.
  Title
The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase.
  Journal
Biol Chem Hoppe Seyler 367:643-57 (1986)
  Sequence
Reference
9  [PMID:3127592]
  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.
  Journal
J Mol Biol 199:525-37 (1988)
DOI:10.1016/0022-2836(88)90623-7
  Sequence
Reference
10 [PMID:2302386]
  Authors
Stoeva S, Kleinschmidt T, Mesrob B, Braunitzer G.
  Title
Primary structure of a zinc protease from Bacillus mesentericus strain 76.
  Journal
Biochemistry 29:527-34 (1990)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.28
IUBMB Enzyme Nomenclature: 3.4.24.28
ExPASy - ENZYME nomenclature database: 3.4.24.28
BRENDA, the Enzyme Database: 3.4.24.28
CAS: 9080-56-2

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