KEGG   ENZYME: 3.4.24.39
Entry
EC 3.4.24.39                Enzyme                                 
Name
deuterolysin;
Penicillium roqueforti protease II;
microbial neutral proteinase II;
acid metalloproteinase;
neutral proteinase II;
Penicillium roqueforti metalloproteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
Reaction(IUBMB)
Preferential cleavage of bonds with hydrophobic residues in P1', also Asn3!Gln and Gly8!Ser bonds in insulin B chain
Comment
Proteolytic activity found in Penicillium roqueforti [4], P. caseicolum [4], Aspergillus sojae [3] and A. oryzae [1,5]. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4
History
EC 3.4.24.39 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.39
Orthology
K19305  deuterolysin
Genes
NCRNCU05071
NTENEUTE1DRAFT113287(NEUTE1DRAFT_113287)
SMPSMAC_07573
MGRMGG_03029 MGG_03808 MGG_07038 MGG_10927 MGG_14981 MGG_15370 MGG_16546 MGG_17758
PPEIPpBr36_02737 PpBr36_09442 PpBr36_09995 PpBr36_10315
PGRIPgNI_10325 PgNI_10999
TMNUCRPA7_5057
FGRFGSG_08289
FPUFPSE_09518
FPOAFPOAC1_004355 FPOAC1_013141 FPOAC1_013503 FPOAC1_013892
FVNFVRRES_04864
FVRFVEG_01804 FVEG_12487
FOXFOXG_02952 FOXG_17405
NHENECHADRAFT_26618 NECHADRAFT_36693 NECHADRAFT_87000
FFCNCS54_00363800 NCS54_00470400 NCS54_00763700 NCS54_01366300
FKRNCS57_00369000 NCS57_00476400 NCS57_00803800 NCS57_01354200
FMUJ7337_007814 J7337_008169
TRETRIREDRAFT_107142
TRRM419DRAFT_78380
MAWMAC_04020 MAC_08853
MAJMAA_00445 MAA_00460 MAA_11285
PCHMVFPPC_02249 VFPPC_05300 VFPPC_09712 VFPPC_16950
CMTCCM_04120 CCM_05691
AMUSLMH87_003420 LMH87_005988 LMH87_006687
PLJVFPFJ_00058 VFPFJ_04289 VFPFJ_05825 VFPFJ_10467 VFPFJ_10638
PTKZJDV02_004622 JDV02_005545 JDV02_008177
VALVDBG_00521 VDBG_01232 VDBG_02494 VDBG_10051
VDAVDAG_00129 VDAG_05354 VDAG_08030
CFJCFIO01_02053 CFIO01_04310 CFIO01_05288 CFIO01_09631 CFIO01_10211 CFIO01_12514
CLUPCLUP02_03101 CLUP02_11559 CLUP02_12150
CHIGCH63R_03475 CH63R_10340 CH63R_11051 CH63R_11582
ELAUCREL1_4917 UCREL1_8793 UCREL1_9503
PFYPFICI_09960 PFICI_12291 PFICI_14897 PFICI_15156
SSLSS1G_08858 SS1G_13741
BFUBCIN_12g06300 BCIN_16g02770(Bcmp1)
GLZGLAREA_03565 GLAREA_05878
ANIANIA_03393 ANIA_07962
AFMAFUA_4G02700 AFUA_4G13750
ACTACLA_052720
NFINFIA_031120 NFIA_102630
AORAO090001000135 AO090005001350 AO090010000493
AFVAFLA_008474 AFLA_013976
ACHEACHE_60090A
APUUAPUU_41596A
PCSN7525_010123
POUPOX_d04876
TRGTRUGW13939_10386
CIMCIMG_00508 CIMG_03010 CIMG_05736 CIMG_07349 CIMG_08613 CIMG_10101 CIMG_11800(CIMG06682)
CPWCPC735_000180 CPC735_001400 CPC735_012270 CPC735_019360 CPC735_031330 CPC735_057220 CPC735_062250
UREUREG_01255 UREG_02006 UREG_03761 UREG_04198
PBLPAAG_11429
PBNPADG_00776
ABEARB_00849 ARB_03949 ARB_04336 ARB_04769 ARB_05817
TVETRV_02539 TRV_03208 TRV_05367 TRV_06370 TRV_07507
AJEHCAG_05788
BGHBDBG_02110 BDBG_03102
PNOSNOG_02177 SNOG_10522
PTEPTT_00390
AALTCC77DRAFT_1000958 CC77DRAFT_1083045
ZTRMYCGRDRAFT_39241
PFJMYCFIDRAFT_189452
FFUCLAFUR5_06567 CLAFUR5_09364
CBETCB0940_02574 CB0940_09444 CB0940_10794
NPAUCRNP2_3253 UCRNP2_4505 UCRNP2_4966
TVSTRAVEDRAFT_164045
ADLAURDEDRAFT_159862 AURDEDRAFT_73421
GTRGLOTRDRAFT_115837 GLOTRDRAFT_64228
CCICC1G_08840 CC1G_12425
ABPAGABI1DRAFT113068(AGABI1DRAFT_113068)
ABVAGABI2DRAFT188701(AGABI2DRAFT_188701)
MPRMPER_00327 MPER_05470 MPER_05717 MPER_07615 MPER_08424 MPER_11500
MRRMoror_11086 Moror_12352 Moror_13478 Moror_13699 Moror_16105 Moror_16682 Moror_2238 Moror_2387 Moror_5075 Moror_5568 Moror_6137 Moror_873 Moror_9829
MOREE1B28_002204 E1B28_004913 E1B28_006265
SCMSCHCO_02009250(SCHCODRAFT_02009250) SCHCO_02509956(SCHCODRAFT_02509956) SCHCO_02598775(SCHCODRAFT_02598775) SCHCO_02609155(SCHCODRAFT_02609155) SCHCO_02620813(SCHCODRAFT_02620813) SCHCO_02670372(SCHCODRAFT_02670372) SCHCO_02688607(SCHCODRAFT_02688607)
WSEWALSEDRAFT_60528
 » show all
Reference
1
  Authors
Nakadai, T., Nasuno, S. and Iguchi, N.
  Title
Purification and properties of neutral proteinase II from Aspergillus oryzae.
  Journal
Agric Biol Chem 37:2703-2708 (1973)
Reference
2  [PMID:4219726]
  Authors
Gripon JC, Hermier J.
  Title
[The proteolytic system of Penicillium roqueforti. III. - Purification, properties and specificity of a protease inhibited by E.D.T.A]
  Journal
Biochimie 56:1323-32 (1974)
Reference
3
  Authors
Sekine, H.
  Title
, Neutral proteinases I and II of Aspergillus sojae action on various substrates.
  Journal
Agric Biol Chem 40:703-709 (1976)
Reference
4  [PMID:6998789]
  Authors
Gripon JC, Auberger B, Lenoir J.
  Title
Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization.
  Journal
Int J Biochem 12:451-5 (1980)
DOI:10.1016/0020-711x(80)90127-5
Reference
5
  Authors
Vaganova, T.I., Ivanova, N.M. and Stepanov, V.M.
  Title
Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae.
  Journal
Biochemistry (Mosc) 53:1171-1178 (1988)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.39
IUBMB Enzyme Nomenclature: 3.4.24.39
ExPASy - ENZYME nomenclature database: 3.4.24.39
BRENDA, the Enzyme Database: 3.4.24.39
CAS: 247028-11-1

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