KEGG   ENZYME: 3.4.21.96Help
Entry
EC 3.4.21.96                Enzyme                                 

Name
lactocepin;
CEP;
extracellular lactococcal proteinase;
lactococcal cell wall-associated proteinase;
lactococcal cell envelope-associated proteinase;
lactococcal proteinase;
PrtP
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position [1,2]. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain
Comment
Associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence. Responsible for the hydrolysis of casein in milk and the provision of peptides essential to cell growth. Important in cheese making and the production of lactic casein, being required for rapid growth to high cell densities with concomitant production of adequate levels of lactic acid. Specificity differences between lactocepins from different starter strains may be partly responsible for imparting different flavour qualities to cheese [4]. In peptidase family S8 (subtilisin family)
History
EC 3.4.21.96 created 1997
Orthology
K01361  lactocepin
Genes
BAG: Bcoa_0671
BIF: N288_23445 N288_23500
BSJ: UP17_23975
BON: A361_04255 A361_13995
BHK: B4U37_19395 B4U37_19815
BKO: CKF48_12445
BMUR: ABE28_022660
OIH: OB2932
OCN: CUC15_17260
GLI: GLN3_08555
HHD: HBHAL_4441(prtB)
VPN: A21D_00884(prtP)
BSE: Bsel_0952
ESI: Exig_2784
EAN: Eab7_2593
GMO: NCTC11323_01630(scpA_2)
JEO: JMA_29650
LLC: LACR_C42
LLI: uc509_p6025(prtP)
SPY: SPy_0416(prtS)
SPYA: A20_0393(prtS)
SPG: SpyM3_0298(prtS)
SPS: SPs1559
SPH: MGAS10270_Spy0340(spyCEP)
SPJ: MGAS2096_Spy0361(spyCEP)
SPK: MGAS9429_Spy0344(spyCEP)
SPF: SpyM51518(prtS)
SPB: M28_Spy0329(prtS)
STG: MGAS15252_0367(scpC)
STX: MGAS1882_0367(scpC)
SOZ: Spy49_0336(prtS)
SPYH: L897_01865
SAG: SAG2053
SAN: gbs2008
SAK: SAK_1991(cspA)
SAGM: BSA_20410
SAGE: EN72_10755
SAGG: EN73_09815
SAGN: W903_1958
STE: STER_0846
STU: STH8232_0989(prtS)
STW: Y1U_C1057
STHE: T303_05205
SSA: SSA_1882(prtS)
SSI: SSU0757(prtS)
SUP: YYK_03620
SST: SSUST3_0948(prtS)
SSUY: YB51_4690
SSK: SSUD12_0974(prtS)
SUI: SSUJS14_0893(prtS)
SUO: SSU12_0755(prtS)
SSUT: TL13_1002(scpC)
SSUI: T15_1146
SGO: SGO_0566(sgc)
SEZ: Sez_0511(scpC)
SEQ: SZO_14810(scpC)
SEQU: Q426_06735
SEU: SEQ_0563(scpC)
SDS: SDEG_0469(cepA) SDEG_0470(cepA)
SDC: SDSE_0487(scpC) SDSE_0488(prtS)
SDQ: SDSE167_0512(cepA) SDSE167_0513(cepA)
SGG: SGGBAA2069_c07210(prtS)
SGT: SGGB_0730
SMB: smi_1398
SOR: SOR_1341
STK: STP_1632
SIF: Sinf_0588
SIE: SCIM_0310(prtS)
SIB: SIR_1402
SIK: K710_1518
LJO: LJ_1840
LAC: LBA1235
LDB: Ldb1189(prtB)
LBU: LBUL_1105
LDE: LDBND_1068(prtB)
LDL: LBU_1015
LCA: LSEI_2270
LPAP: LBPC_2201
LCB: LCABL_24520(prtP)
LCS: LCBD_2450
LCE: LC2W_2433
LCW: BN194_24060(prtP)
LHL: LBHH_1000
LHV: lhe_1828
LHD: HUO_05935
LRH: LGG_02274(prtP)
LRG: LRHM_2185
LRL: LC705_02265(prtP)
LRA: LRHK_2273(prtP)
LAM: LA2_06960
LKE: WANG_0583
CML: BN424_3077(prtB)
CPF: CPF_1123
CPR: CPR_0968(prtP)
CBN: CbC4_1800
BPB: bpr_I2629
BFI: CIY_15260
THX: Thet_2357
TKI: TKV_c23360(amyB)
FMA: FMG_0035
PMIC: NW74_00080
ERH: ERH_0260
AHE: Arch_1015
TPYO: X956_03895
SIJ: SCIP_0787
PDO: PSDT_1426
CBAC: JI75_01655
CEX: CSE_15380
 » show all
Taxonomy
Reference
1  [PMID:1367552]
  Authors
Visser S, Robben AJ, Slangen CJ.
  Title
Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine beta-casein.
  Journal
Appl Microbiol Biotechnol 35:477-83 (1991)
Reference
2  [PMID:1592148]
  Authors
Monnet V, Ley JP, Gonzalez S.
  Title
Substrate specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763.
  Journal
Int J Biochem 24:707-18 (1992)
Reference
3  [PMID:8285671]
  Authors
Exterkate FA, Alting AC, Bruinenberg PG.
  Title
Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.
  Journal
Appl Environ Microbiol 59:3640-7 (1993)
Reference
4  [PMID:8398214]
  Authors
Pritchard GG, Coolbear T.
  Title
The physiology and biochemistry of the proteolytic system in lactic acid bacteria.
  Journal
FEMS Microbiol Rev 12:179-206 (1993)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.96
IUBMB Enzyme Nomenclature: 3.4.21.96
ExPASy - ENZYME nomenclature database: 3.4.21.96
BRENDA, the Enzyme Database: 3.4.21.96
CAS: 205510-58-3

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