Information on EC 3.4.21.96 - Lactocepin

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.4.21.96
-
RECOMMENDED NAME
GeneOntology No.
Lactocepin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain
show the reaction diagram
endopeptidase
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cell envelope associated proteinase
-
-
cell envelope proteinase
-
-
cell envelope proteinase
Lactobacillus helveticus Zuc2
-
-
-
cell envelope proteinase
-
-
cell envelope proteinase
Lactococcus lactis s4
-
-
-
cell wall anchored proteinase
-
-
Cell wall-associated serine proteinase
-
-
-
-
cell-bound cell envelope proteinase
-
-
Cell-envelope proteinase
-
-
-
-
Cell-envelope-located serine proteinase
-
-
-
-
Cell-wall-bound proteinase
-
-
-
-
CEP
-
-
-
-
CEP
Lactobacillus helveticus Zuc2
-
-
-
Extracellular lactococcal proteinase
-
-
-
-
Lactocepin
-
-
-
-
Lactocepin I
-
-
-
-
Lactocepin I
-
-
lactococcal cell envelope proteinase
-
-
Lactococcal cell envelope-associated proteinase
-
-
-
-
Lactococcal cell wall-associated proteinase
-
-
-
-
Lactococcal PI-type proteinase
-
-
Lactococcal PIII-type poteinase
-
-
Lactococcal proteinase
-
-
-
-
Lactococcal proteinase PI
-
-
Lactococcal proteinase PI
Lactococcus lactis SK11
-
-
-
LP151
-
-
-
-
PrtH
-
Lactobacillus helveticus can possess one or two cell envelope proteinases called PrtH2 and PrtH
PrtH2
-
Lactobacillus helveticus can possess one or two cell envelope proteinases called PrtH2 and PrtH
PrtP
-
-
-
-
PrtP proteinase
-
-
CAS REGISTRY NUMBER
COMMENTARY
205510-58-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
subsp. lactis CRL 581
-
-
Manually annotated by BRENDA team
a diversity of 15 strains of Lactobacillus helveticus are explored in terms of their proteolytic activities and specificities on pure caseins or on milk casein micelles. CEP activity differ 14fold when the strains are assayed on a synthetic substrate, but no significant differences are detected between strains possessing one or two CEPs. Simultaneous presence of PrtH and PrtH2 proteinases in Lactobacillus helveticus strains improves breakdown of the pure alphas1-casein
-
-
Manually annotated by BRENDA team
strain Zuc2, from natural whey culture for Grana Padano cheese
-
-
Manually annotated by BRENDA team
Lactobacillus helveticus Zuc2
strain Zuc2, from natural whey culture for Grana Padano cheese
-
-
Manually annotated by BRENDA team
subsp. paracasei NCDO 151
-
-
Manually annotated by BRENDA team
strains BGT43, BGT51-K, BGT54-K, BGT110, BGT266, BGT389, BGT390, BGT391, BGT392, BGT393, BGT394, BGT805, BGRI7, BGZL7, BGZL18, BGZL19, BGZL20, ATCC7469, CRL1036, CRL536 and EN1
-
-
Manually annotated by BRENDA team
SK11; strain AM2; strain C13; strain E8; strain FD21; strain H61; strain HP; strain K14; strain UC317; strain US3; strain Wg2; strain Z8; subsp. cremoris strain AM1; subsp. lactis NCDO 763
-
-
Manually annotated by BRENDA team
strain S4, commercial cheese starter culture, group h lactocepin
-
-
Manually annotated by BRENDA team
subsp. cremoris BC 101
-
-
Manually annotated by BRENDA team
subsp. cremoris SK11
-
-
Manually annotated by BRENDA team
subsp. cremoris SK11, subsp. cremoris Wg2, MG1363
-
-
Manually annotated by BRENDA team
subsp. cremoris strain AM1
-
-
Manually annotated by BRENDA team
subsp. cremoris strain AM1; subsp. cremoris strain HM
-
-
Manually annotated by BRENDA team
subsp. lactis and subsp. cremonis H2
-
-
Manually annotated by BRENDA team
subsp. lactis BN1
-
-
Manually annotated by BRENDA team
subsp. lactis MG611
-
-
Manually annotated by BRENDA team
subsp. lactis NCDO 763
-
-
Manually annotated by BRENDA team
Lactococcus lactis AM2
strain AM2
-
-
Manually annotated by BRENDA team
Lactococcus lactis C13
strain C13
-
-
Manually annotated by BRENDA team
Lactococcus lactis E8
strain E8
-
-
Manually annotated by BRENDA team
Lactococcus lactis FD21
strain FD21
-
-
Manually annotated by BRENDA team
Lactococcus lactis H61
strain H61
-
-
Manually annotated by BRENDA team
Lactococcus lactis HP
strain HP
-
-
Manually annotated by BRENDA team
Lactococcus lactis K14
strain K14
-
-
Manually annotated by BRENDA team
Lactococcus lactis s4
strain S4, commercial cheese starter culture, group h lactocepin
-
-
Manually annotated by BRENDA team
Lactococcus lactis SK11
SK11
-
-
Manually annotated by BRENDA team
Lactococcus lactis UC317
strain UC317
-
-
Manually annotated by BRENDA team
Lactococcus lactis US3
strain US3
-
-
Manually annotated by BRENDA team
Lactococcus lactis Wg2
strain Wg2
-
-
Manually annotated by BRENDA team
Lactococcus lactis Z8
strain Z8
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha(S1)-casein + H2O
?
show the reaction diagram
-, Q49SG9, Q49SH0
-
-
-
?
alpha1-casein + H2O
Fragments of alpha1-casein
show the reaction diagram
-
-
-
-
?
alpha1-casein + H2O
fragments of alphas1-casein
show the reaction diagram
-
-
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
-
-
-
-
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
-
-
-
-
-
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
-
-
the product spectrum depends on water activity and salt concentration
-
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
-
specificity of the enzyme for the Arg22-Phe23 bond
-
-
?
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
Lactococcus lactis SK11
-
-
-
-
-
alphas1-Casein + H2O
Fragments of alphas1-casein
show the reaction diagram
Lactobacillus helveticus Zuc2
-
specificity of the enzyme for the Arg22-Phe23 bond
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-
-
-
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-, Q49SG9, Q49SH0
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-
the wild-type enzyme of strain SK11, cleaves bonds 16-17 and 17-18, the mutant enzyme lacking the loop 238-388 is highly specific for bond 21-22
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-
PI-type proteinase of subsp. cremoris strain HP cleaves the bonds 8-9, 9-10, 13-14, the PIII- type proteinase of subsp. cremoris strain AM1 cleaves bonds 16-17, 17-18, 21-22
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
-
specificity of the enzyme for Lys3-His4 bond
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis s4
-
-
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis US3, Lactococcus lactis HP, Lactococcus lactis H61, Lactococcus lactis Wg2, Lactococcus lactis FD21, Lactococcus lactis AM2, Lactococcus lactis K14, Lactococcus lactis E8
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis SK11
-
the wild-type enzyme of strain SK11, cleaves bonds 16-17 and 17-18, the mutant enzyme lacking the loop 238-388 is highly specific for bond 21-22
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis SK11
-
-
-
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis SK11
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
-
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactobacillus helveticus Zuc2
-
specificity of the enzyme for Lys3-His4 bond
-
-
?
alphas1-Casein fragment 1-23 + H2O
Fragments of alphas1-casein fragment 1-23
show the reaction diagram
Lactococcus lactis C13, Lactococcus lactis UC317, Lactococcus lactis Z8
-
the strains of Lactococcus lactis can be devided into seven groups according to the cleavage pattern of this substrate: strains US3, AM1, SK11 possess PIII-type proteinases, strains WG2, C13, K14, Z8, H61, FD21, HP possess PI-type proteinases, strains E8, AM2, NCDO 763, UC 317 possess proteinases of an intermediate type
-
-
-
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
-
-
-
-
-
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
-
-
-
-
?
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
-
-
subsp. lactis MG611, more than 100 different fragments
-
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
-
PIII-type proteinase of subsp. cremoris AM1 preferentially cleaves 16 peptide bonds, the cleavage sites are primarily Gln-X or Glu-X, mostly a large hydrophobic residue is part of the cleavable position, a hydrophobic residue is frequently at position P2, sometimes also at P2', one or more side chains in P2-P3 or P2'-P3' are negetively charged
-
-
-
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
-
shows proteolytic activity only under in vivo conditions
-
-
?
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
Lactococcus lactis SK11
-
-
-
-
-
beta-Casein + H2O
Fragments of beta-casein
show the reaction diagram
Lactobacillus helveticus Zuc2
-
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
hydrolysis of alpha-s1-, beta- and kappa-casein, alpha-s1-casein which is normally resistant to lactocepin I activity is rapidly hydrolyzed in presence of polyethylene glycol 20000
-
?
casein + H2O
?
show the reaction diagram
-
nitrogen nutrition mechanism of lactic streptococci, process in cheese ripening
-
-
-
Insulin B-chain + H2O
Fragments of insulin B-chain
show the reaction diagram
-
-
-
-
kappa-Casein + H2O
Fragemnts of kappa-casein
show the reaction diagram
-
-
-
-
-
kappa-casein + H2O
fragments of kappa-casein
show the reaction diagram
Lactobacillus helveticus, Lactobacillus helveticus Zuc2
-
specificity of the enzyme for Phe105-Met106 bond
-
-
?
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
show the reaction diagram
Lactococcus lactis US3, Lactococcus lactis HP, Lactococcus lactis H61, Lactococcus lactis Wg2, Lactococcus lactis FD21, Lactococcus lactis AM2, Lactococcus lactis K14, Lactococcus lactis E8
-
-
-
-
-
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
show the reaction diagram
Lactococcus lactis SK11
-
-
-
-
-
Suc-Ala-Glu-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
Lactococcus lactis, Lactococcus lactis US3, Lactococcus lactis HP, Lactococcus lactis H61, Lactococcus lactis Wg2, Lactococcus lactis FD21, Lactococcus lactis AM2, Lactococcus lactis K14, Lactococcus lactis E8, Lactococcus lactis SK11, Lactococcus lactis C13, Lactococcus lactis UC317, Lactococcus lactis Z8
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
synthetic substrate
-
-
?
Succinyl-Ala-Glu-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Glu-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
Lactococcus lactis SK11
-
-
-
-
-
Succinyl-Ala-Gly-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-His-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ile-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Leu-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Lys-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Phe-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Trp-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
succinyl-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
synthetic substrate
-
-
?
Usp 45 + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis SK11
-
a secreted 60 kDa protein of Lactococcus lactis
-
-
-
Methoxysuccinyl-Arg-Pro-Tyr 4-nitroanilide + H2O
?
show the reaction diagram
Lactococcus lactis C13, Lactococcus lactis UC317, Lactococcus lactis Z8
-
-
-
-
-
additional information
?
-
-
overview, specificity of wild-type SK11 proteinase and its mutants as compared to strain Wg2
-
-
-
additional information
?
-
-
subsp. lactis NCDO 763 prefers hydrophilic amino acids in P4, proline in P2 and hydrophilic amino acids in P1
-
-
-
additional information
?
-
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
-
PI-type proteinase hydrolyzes beta- casein and kappa-casein, PIII-type proteinase hydrolyzes beta-casein and kappa-caein with different bond-specificities and alpahs1-casein
-
-
-
additional information
?
-
Lactococcus lactis US3
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis HP
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis H61
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis Wg2
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis FD21
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis AM2
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis K14
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis E8
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis SK11
-
overview, specificity of wild-type SK11 proteinase and its mutants as compared to strain Wg2
-
-
-
additional information
?
-
Lactococcus lactis SK11
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis C13
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis UC317
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
additional information
?
-
Lactococcus lactis Z8
-
comparison of the amino acid sequences of the substrate-binding regions, the activity of PIII-type proteinases increases with the hydrophobicity of the P3-side chain, PI-type proteinases have the lowest activity with Glu at P3
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
nitrogen nutrition mechanism of lactic streptococci, process in cheese ripening
-
-
-
Usp 45 + H2O
?
show the reaction diagram
Lactococcus lactis, Lactococcus lactis SK11
-
a secreted 60 kDa protein of Lactococcus lactis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
triggers stabilization, removal of weakly bound Ca2+ from the native cell-bound enzyme is coupled with a significant reversible decrease in specific activity and a dramatic reversible reduction in thermal stability
Cd2+
-
can replace Ca2+
additional information
-
Mn2+ is much less efficient, Zn2+, Mg2+, Ba2+, Ni2+, Co2+, Cu2+, and Sn2+ have no significant effect
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3,4-Dichloroisocoumarin
-
complete and irreversible inhibition with 0.1 mM
alpha-casein
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of alpha-casein CEP activity is inhibited 1fold
-
beta-casein
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of beta-casein CEP activity is inhibited 1.2fold
-
branched-chain amino acids
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of branched-chain amino acids CEP activity is inhibited 1.7fold
-
casamino acid
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of casamino acid 1% (w,v) or 0.2% (w,v) CEP activity is inhibited 70fold or 20fold, respectively
-
casitone
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of casitone 1% (w,v) or 2% (w,v) CEP activity is inhibited 99fold or 51fold, respectively
-
glycerol
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of glycerol CEP activity is inhibited 1.3fold
leucylglycylglycine
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of leucylglycylglycine 1 mM or 5 mM, CEP activity is inhibited 6.5fold or 12.9fold, respectively
leucylleucine
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of leucylleucine 1 mM or 5 mM, CEP activity is inhibited 7.2fold or 15.1fold, respectively
leucylproline
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of leucylproline 1 mM or 5 mM, CEP activity is inhibited 4fold or 8.8fold, respectively
NaCl
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of NaCl 0.25%-1% (w, u) CEP activity is inhibited 1.4fold
Pepstatin
-
1 mM inhibits approximately 10%, enzyme activity is almost completely restored after inhibitor removal
PMSF
-
complete and irreversible inhibition with 1 mM
prolylleucine
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of prolylleucine 1 mM or 5 mM, CEP activity is inhibited 3.5fold or 9.9fold, respectively
yeast extract
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of yeast extract CEP activity is inhibited 68fold
-
low-molecular-mass peptides
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of low-molecular-mass peptides 1% (w, u) CEP activity is inhibited 99fold
-
additional information
-
no inhibition with the thiol-proteinase inhibitor E-64
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
the CEP activity levels are controlled by the peptide content of the growth medium. The maximum activity is observed in a basal minimal defined medium
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
6
-
Ca-free enzyme
6.4
-
-
Ca-loaded enzyme
6.5
-
-
efficient degradation of beta-casein
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
7
-
Ca-free enzyme
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Lactobacillus helveticus Zuc2, Lactococcus lactis AM2, Lactococcus lactis C13, Lactococcus lactis E8, Lactococcus lactis FD21, Lactococcus lactis H61, Lactococcus lactis HP, Lactococcus lactis K14, Lactococcus lactis SK11, Lactococcus lactis UC317, Lactococcus lactis US3, Lactococcus lactis Wg2, Lactococcus lactis Z8
-
-
-
Manually annotated by BRENDA team
additional information
-
in comparison to other CEPs, the PrtP proteinase does not have the same mechanism of release from the cell surface
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72000
-
-
SDS-PAGE
145000
-
-
Ca-free enzyme, gel filtration
150000
-
-
gel filtration, enzyme pro110
150000
-
-
gel filtration
180000
-
-
mature active enzyme
250000
-
-
gel filtration
300000
-
-
gel filtration, enzyme pro135
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
strain SK11, autoproteolysis yields fragments of 120000, 82000, 50000; strain SK11, x * 145000, SDS-PAGE
?
-
strain SK11, x * 145000, SDS-PAGE; strain SK11, x * 200000, inactive, unprocessed precursor of an active-site mutant
?
-
x * 180000, SDS-PAGE
?
Lactobacillus helveticus Zuc2
-
x * 180000, SDS-PAGE
-
?
Lactococcus lactis SK11
-
strain SK11, autoproteolysis yields fragments of 120000, 82000, 50000; strain SK11, x * 145000, SDS-PAGE; strain SK11, x * 145000, SDS-PAGE; strain SK11, x * 200000, inactive, unprocessed precursor of an active-site mutant
-
dimer
-
2 * 135000, SDS-PAGE
dimer
-
subsp. cremoris BC101, 2 * 150000, SDS-PAGE
monomer
-
1 * 110000, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
Ca-free cell-bound enzyme is extremely unstable, lose 99% of its potential activity within 20 min
37
60
-
retains 40% of activity when incubated for 2 h at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0°C, Ca-free enzyme, storage on ice results in a gradual loss of potential activity, 20% reduction in activity after 4 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by gel filtration and ion-exchange chromatography, 527.42fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant MG 1363 strains containg plasmid-located hybrid proteinase genes constructed from SK11 and Wg2
-
stain SK11, cloned in Lactococcus lactis strains MG1363 and SK1128
-
subsp. lactis MG611, carrying the genes prtP and prtM of subsp. cremoris Wg2 on its chromosome
-
the enzyme of subsp. cremoris WG2 and strain SK11 are plasmid-encoded, the enzyme of subsp. cremoris BC101 is chromosomally -encoded
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
in strain SK11 deletion of the largest loop, a fragment of amino acids 238-388 yields a mutant with a 2fold reduced activity
additional information
-
in strain SK11 the mutagenesis of the loop 205-219 region of the catalytic domain results in inactivation, mostly due to inhibiton of autoprocessing of proenzyme
additional information
-, Q49SG9, Q49SH0
prtP replacement mutants (strains S3 or S4 with altered lactocepin gene sequence) have a slower rate of acidification than parental strains after 2.5 or 5 h incubation in ultra high temperature skim milk
additional information
Lactococcus lactis s4
-
prtP replacement mutants (strains S3 or S4 with altered lactocepin gene sequence) have a slower rate of acidification than parental strains after 2.5 or 5 h incubation in ultra high temperature skim milk
-
additional information
Lactococcus lactis SK11
-
in strain SK11 deletion of the largest loop, a fragment of amino acids 238-388 yields a mutant with a 2fold reduced activity; in strain SK11 the mutagenesis of the loop 205-219 region of the catalytic domain results in inactivation, mostly due to inhibiton of autoprocessing of proenzyme
-
additional information
-
strain PRTP- exhibits very low affinity for mono-polar solvents chloroform and ethyl acetate and apolar solvents hexadecane and decane (maximal affinity less than 20%), independently of their different physico-chemical properties (whether apolar, Lewis-acid or Lewis-base). Strain PRTP*, encoding anchored inactive PrtP, exhibits higher affinity to all solvents. More efficient adhesion of PRTP* strain to solid (glass and polytetrafluorethylene) surfaces as compared to PRTP+ strain
additional information
-
using isogenic Msp and PrtP protease complex mutant strains and wild-type strains. It is shown that human serum antibodies recognize Treponema denticola Msp and PrtP protease complex proteins
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-, Q49SG9, Q49SH0
conversion of lactocepin substrate binding regions by allele exchange can effectively alter lactocepin specificity in industrial strains of Lactococcus lactis without significantly affecting other important strain properties. The methodology can be used to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect; conversion of lactocepin substrate binding regions by allele exchange can effectively alter lactocepin specificity in industrial strains of Lactococcus lactis without significantly affecting other important strain properties. The methodology can be used to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect
industry
-, Q49SG9, Q49SH0
method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate
nutrition
-
cheese making, cheese starter organism, dairy industry
industry
Lactococcus lactis s4
-
method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate
-
additional information
-
exposure of PrtP, and not its proteolytic activity, is responsible for greater cell hydrophobicity and adhesion. The increased bacterial affinity to polar and apolar solvents indicates that exposure of PrtP on lactococcal cell surface can enhance the capacity to exchange attractive van der Waals interactions, and consequently increase their adhesion to different types of solid surfaces and solvents. PrtP or its derivatives may be used as a tool to construct strains with increased adhesion that form protective biofilms