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Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
Ala-Pro-Arg + H2O
Ala-Pro + Arg
Ala-Pro-Gly + H2O
Ala-Pro + Gly
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
Arg-Pro-Ala + H2O
Arg-Pro + Ala
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
-
-
-
-
?
beta-casein + H2O
?
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Ala-7-amido-4-methylcoumarin + H2O
Gly-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
Gly-Pro-Ala + H2O
Gly-Pro + Ala
Gly-Pro-Arg-Pro + H2O
Gly-Pro + Arg-Pro
-
as active as Gly-Pro-4-nitroanilide
-
-
?
Gly-Pro-Gly-Gly + H2O
Gly-Pro + Gly-Gly
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
His-Pro-Leu + H2O
His-Pro + Leu
-
-
-
-
?
His-Pro-Tyr + H2O
His-Pro + Tyr
-
-
-
-
?
Ile-Pro-Ile + H2O
Ile-Pro + Ile
-
34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
L-Ala-L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
L-Ala-L-Pro-L-Arg + H2O
L-Ala-L-Pro + L-Arg
L-Ala-L-Pro-L-Ser + H2O
L-Ala-L-Pro + L-Ser
L-Ala-L-Pro-L-Tyr + H2O
L-Ala-L-Pro + L-Tyr
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
L-Arg-L-Pro-L-Ala + H2O
L-Arg-L-Pro + L-Ala
-
-
-
?
L-Asp-L-Pro-L-Ala + H2O
L-Asp-L-Pro + L-Ala
-
-
-
?
L-Ser-L-Pro-L-Ala + H2O
L-Ser-L-Pro + L-Ala
-
-
-
?
L-Tyr-L-Pro-L-Ala + H2O
L-Tyr-L-Pro + L-Ala
-
-
-
?
Leu-Ala-Pro + H2O
?
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
Lys-Ala-Val-Pro-Tyr-Pro-Gln + H2O
?
-
fragment 176-182 of beta-casein
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
-
85% of the activity with Arg-Pro-p-nitroanilide
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Pro-Phe-Pro-Gly-Pro-Ile + H2O
Pro-Phe + Pro-Gly-Pro-Ile
-
-
-
-
?
Ser-Pro-Ala + H2O
Ser-Pro + Ala
Tyr-Pro-Ala + H2O
Tyr-Pro + Ala
Tyr-Pro-Phe + H2O
Tyr-Pro + Phe
-
-
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr-Pro + Phe-Pro-Gly-Pro-Ile
-
i.e. BCM-7, beta-casomorphin 7
-
-
?
Val-Pro-Leu + H2O
Val-Pro + Leu
-
83% of the activity with Gly-Pro-nitroanilide
-
-
?
additional information
?
-
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
2% of the activity with Gly-Pro 4-nitroanilide
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
?
Ala-Pro-Arg + H2O
Ala-Pro + Arg
-
-
-
?
Ala-Pro-Arg + H2O
Ala-Pro + Arg
-
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
11% of the activity with Gly-Pro 4-nitroanilide
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
72% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
best substrate
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
130% of the activity with Gly-Pro 4-nitroanilide
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
60.5% of the activity with Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
55% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro-Ala + H2O
Arg-Pro + Ala
-
-
-
?
Arg-Pro-Ala + H2O
Arg-Pro + Ala
-
-
-
?
beta-casomorphin + H2O
?
-
-
the hydrolysis of the tripeptide Gly-Pro-Ile is slower, after the release of the dipeptide Tyr-Pro, the resulting pentapeptide does not accumulate in the medium, rather the dipeptide Phe-Pro is released very rapidly
?
beta-casomorphin + H2O
?
-
-
main split products: Tyr-Pro and Phe-Pro
?
beta-casomorphin + H2O
?
-
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
the hydrolysis of the tripeptide Gly-Pro-Ile is slower, after the release of the dipeptide Tyr-Pro, the resulting pentapeptide does not accumulate in the medium, rather the dipeptide Phe-Pro is released very rapidly
?
beta-casomorphin + H2O
?
-
fragment 60-66 of beta-casein or beta-casomorphin
main split products: Tyr-Pro, Phe-Pro and Gly-Pro-Ile
?
beta-casomorphin + H2O
?
-
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
the hydrolysis of the tripeptide Gly-Pro-Ile is slower
?
beta-casomorphin + H2O
?
-
-
main split products: Tyr-Pro and Phe-Pro
?
beta-casomorphin + H2O
?
-
-
main split products: Tyr-Pro and Phe-Pro
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
6% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
6% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
-
16% of the activity with L-Ala-L-Pro 4-nitroanilide
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
25.5% of the activity with Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly-Pro + Ala
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly-Pro + Ala
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
Lacticaseibacillus casei Lc 279
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
best substrate
-
-
?
L-Ala-L-Pro-L-Arg + H2O
L-Ala-L-Pro + L-Arg
-
-
-
?
L-Ala-L-Pro-L-Arg + H2O
L-Ala-L-Pro + L-Arg
-
-
-
?
L-Ala-L-Pro-L-Ser + H2O
L-Ala-L-Pro + L-Ser
-
-
-
?
L-Ala-L-Pro-L-Ser + H2O
L-Ala-L-Pro + L-Ser
-
-
-
?
L-Ala-L-Pro-L-Tyr + H2O
L-Ala-L-Pro + L-Tyr
-
-
-
?
L-Ala-L-Pro-L-Tyr + H2O
L-Ala-L-Pro + L-Tyr
-
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
59% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
59% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
-
13.6% of the activity with L-Ala-L-Pro 4-nitroanilide
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
9.9% of the activity with Gly-Pro-7-amido-4-methylcoumarin
-
-
?
Ser-Pro-Ala + H2O
Ser-Pro + Ala
-
-
-
?
Ser-Pro-Ala + H2O
Ser-Pro + Ala
-
-
-
?
Tyr-Pro-Ala + H2O
Tyr-Pro + Ala
-
-
-
?
Tyr-Pro-Ala + H2O
Tyr-Pro + Ala
-
-
-
?
VYPFPGPIPN + H2O
?
substrate opioid precursor peptide, which is released during casein hydrolysis
-
-
?
VYPFPGPIPN + H2O
?
substrate opioid precursor peptide, which is released during casein hydrolysis
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
-
no activity with Ala-Leu-Ala
-
-
?
additional information
?
-
no substrate inhibition is determined
-
-
?
additional information
?
-
no substrate inhibition is determined
-
-
?
additional information
?
-
-
no activity with Ala-Leu-Ala
-
-
?
additional information
?
-
-
no activity with bradikinins with N-terminal sequences Arg-Pro-Pro- and Lys-Pro-Pro-
-
-
?
additional information
?
-
-
no activity with Pro-p-nitroanilide or azocasein
-
-
?
additional information
?
-
-
maximal activity with Pro in the N-penultimate position
-
-
?
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Khalid, N.M.; Marth, E.H.
Purification and partial characterization of a prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ 32
Appl. Environ. Microbiol.
56
381-388
1990
Lactobacillus helveticus, Lactobacillus helveticus CNRZ 32
brenda
Tsakalidou, E.; Anastasiou, R.; Papadimitriou, K.; Manopoulou, E.; Kalantzopoulos, G.
Purification and characterisation of an intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococus thermophilus ACA-DC 4
J. Biotechnol.
59
203-211
1997
Streptococcus thermophilus, Streptococcus thermophilus ACA-DC 4
brenda
Kiefer-Partsch, B.; Bockelmann, W.; Geis, A.; Teuber, M.
Purification of an X-prolyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. Cremoris
Appl. Microbiol. Biotechnol.
31
75-78
1989
Lactococcus lactis, Lactococcus lactis P8-2-47, Lactococcus lactis subsp. cremoris
-
brenda
Yan, T.R.; Ho, S.C.; Hou, C.L.
Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR
Biosci. Biotechnol. Biochem.
56
704-707
1992
Lactococcus lactis, Lactococcus lactis nTR, Lactococcus lactis subsp. cremoris
brenda
Chich, J.F.; Rigolet, P.; Nardi, M.; Gripon, J.C.; Ribadeau-Dumas, B.; Brunie, S.
Purification, crystallization, and preliminary X-ray analysis of PepX, an X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
Proteins Struct. Funct. Genet.
23
278-281
1995
Lactococcus lactis, Lactococcus lactis NCDO 763
brenda
Habibi-Najafi, M.B.; Lee, B.H.
Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG
Appl. Microbiol. Biotechnol.
42
280-286
1994
Lacticaseibacillus casei, Lacticaseibacillus casei LLG
brenda
Zevaco, C.; Monnet, V.; Gripon, J.C.
Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties
J. Appl. Bacteriol.
68
357-366
1990
Lactococcus lactis, Lactococcus lactis NCDO 763
-
brenda
Miyakawa, H.; Hashimoto, I.; Nakamura, T.; Ishibashi, N.; Shimamura, S.; Igoshi, K.
Purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus helveticus LHE-511
Milchwissenschaft
49
670-673
1994
Lactobacillus helveticus, Lactobacillus helveticus LHE-511
-
brenda
Lloyd, R.J.; Pritchard, G.G
Characterization of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. Lactis
J. Gen. Microbiol.
137
49-55
1991
Lactococcus lactis, Lactococcus lactis H1
-
brenda
Chich, J.F.; Chapot-Chartier, M.P.; Ribadeau-Dumas, B.; Gripon, J.C.
Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
FEBS Lett.
314
139-142
1992
Lactococcus lactis
brenda
Chich, J.F.; Gripon, J.C.; Ribadeau-Dumas, B.
Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents
Anal. Biochem.
224
245-249
1995
Lactococcus lactis
brenda
Meyer-Barton, E.C.; Klein, J.R.; Imam, M.; Plapp, R.
Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbruckii ssp. lactis DSM7290
Appl. Microbiol. Biotechnol.
40
82-89
1993
Lactobacillus delbrueckii
brenda
Tachi, H.; Ito, H.; Ichishima, E.
An X-prolyl dipeptidyl-aminopeptidase from Aspergillus oryzae
Phytochemistry
31
3707-3709
1992
Aspergillus oryzae
-
brenda
Vesanto, E.; Savijoki, K.; Rantanen, T.; Steele, J.L.; Palva, A.
An X-prolyl dipeptidyl aminopeptidase (pepX) gene from Lactobacillus helveticus
Microbiology
141
3067-3075
1995
Lactobacillus helveticus, Lactobacillus helveticus 53/7
brenda
El Abboudi, M.; El Soda, M.; Pandian, S.; Simard, R.E.; Olson, N.F.
Purification of X-prolyl dipeptidyl aminopeptidase from Lactobacillus casei subspecies
Int. J. Food Microbiol.
15
87-98
1992
Lacticaseibacillus casei, Lacticaseibacillus casei UL21, Lacticaseibacillus casei UL26
brenda
Bockelmann, W.; Fobker, M.; Teuber, M.
Purification and characterization of the X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus and Lactobacillus acidophilus
Int. Dairy J.
1
51-66
1991
Lactobacillus acidophilus, Lactobacillus delbrueckii
-
brenda
Miyakawa, H.; Kobayashi, S.; Shimamura, S.; Tomita, M.
purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus delbrueckii ssp. bulgaricus LBU-147
J. Dairy Sci.
74
2375-2381
1991
Lactobacillus delbrueckii, Lactobacillus delbrueckii LBU-147
-
brenda
Meyer, J.; Jordi, R.
Purification and characterization of X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus lactis and from Streptococcus thermophilus
J. Dairy Sci.
70
738-745
1987
Lactobacillus delbrueckii subsp. lactis, Streptococcus thermophilus
brenda
Rigolet, P.; Mechin, I.; Delage, M.M.; Chich, J.F.
The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
Structure
10
1383-1394
2002
Lactococcus lactis (P22346)
brenda
Sanz, Y.; Toldra, F.
Purification and characterization of an X-prolyl-dipeptidyl peptidase from Lactobacillus sakei
Appl. Environ. Microbiol.
67
1815-1820
2001
Latilactobacillus sakei
brenda
Rigolet, P.; Xi, X.G.; Rety, S.; Chich, J.F.
The structural comparison of the bacterial PepX and human DPP-IV reveals sites for the design of inhibitors of PepX activity
FEBS J.
272
2050-2059
2005
Lactococcus lactis (P22346)
brenda
Gallo, G.; De Angelis, M.; McSweeney, P.L.; Corbo, M.R.; Gobbetti, M.
Partial purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus sanfranciscensis CB1
Food Chem.
91
535-544
2005
Fructilactobacillus sanfranciscensis, Fructilactobacillus sanfranciscensis CB1
brenda
Gatti, M.; Fornasari, M.E.; Lazzi, C.; Mucchetti, G.; Neviani, E.
Peptidase activity in various species of dairy thermophilic lactobacilli
J. Appl. Microbiol.
96
223-229
2004
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. lactis, Lactobacillus helveticus
brenda
Perez-Gutman, A.E.; Cruz y Victoria, T.; Cruz-Camarillo, R.; Hernandez-Sanchez, H.
Improvement of fermentation conditions for the production of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis
World J. Microbiol. Biotechnol.
20
413-417
2004
Lactococcus lactis subsp. lactis, Lactococcus cremoris
-
brenda
Donkor, O.N.; Henriksson, A.; Vasiljevic, T.; Shah, N.P.
Proteolytic activity of dairy lactic acid bacteria and probiotics as determinant of growth and in vitro angiotensin-converting enzyme inhibitory activity in fermented milk
Lait
87
21-38
2007
Bifidobacterium longum, Lactobacillus acidophilus, Lacticaseibacillus casei, Lactobacillus delbrueckii, Streptococcus thermophilus, Bifidobacterium animalis subsp. lactis, Bifidobacterium animalis subsp. lactis B94, Lacticaseibacillus casei L26, Lactobacillus acidophilus L10, Bifidobacterium longum BI 536, Streptococcus thermophilus St 1342, Lacticaseibacillus casei Lc 279, Lactobacillus acidophilus La 4962
-
brenda
Perez-Guzman, A.E.; Cruz y Victoria, T.; Cruz-Camarillo, R.; Hernandez-Sanchez, H.
Purification and characterization of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris NRRL 634
World J. Microbiol. Biotechnol.
22
953-958
2006
Lactococcus lactis
-
brenda
Bachmann, H.; Starrenburg, M.J.; Dijkstra, A.; Molenaar, D.; Kleerebezem, M.; Rademaker, J.L.; van Hylckama Vlieg, J.E.
Regulatory phenotyping reveals important diversity within the species Lactococcus lactis
Appl. Environ. Microbiol.
75
5687-5694
2009
Lactococcus lactis, Lactococcus lactis (P22346)
brenda
Juarez-Montiel, M.; Ibarra, J.A.; Chavez-Camarillo, G.; Hernandez-Rodriguez, C.; Villa-Tanaca, L.
Molecular cloning and heterologous expression in Pichia pastoris of X-prolyl-dipeptidyl aminopeptidase from basidiomycete Ustilago maydis
Appl. Biochem. Biotechnol.
172
2530-2539
2014
Ustilago maydis
brenda
Stressler, T.; Eisele, T.; Kranz, B.; Fischer, L.
PepX from Lactobacillus helveticus: Automated multi-step purification and determination of kinetic parameters with original tripeptide substrates
J. Mol. Catal. B
108
103-110
2014
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 12046 (S4TJ23)
-
brenda
Stressler, T.; Eisele, T.; Schlayer, M.; Lutz-Wahl, S.; Fischer, L.
Characterization of the recombinant exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 important for food protein hydrolysis
PLoS ONE
8
e70055
2013
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 120460 (S4TJ23)
brenda
Stressler, T.; Ewert, J.; Eisele, T.; Fischer, L.
Cross-linked enzyme aggregates (CLEAs) of PepX and PepN - production, partial characterization and application of combi-CLEAs for milk protein hydrolysis
Biocatal. Agricult. Biotechnol.
4
752-760
2015
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 12046 (S4TJ23)
-
brenda
Braun, C.; Ewert, J.; Stressler, T.
Characterization of cross-linked enzyme aggregates (CLEAs) of the fusion protein FUS-PepN_PepX and their application for milk protein hydrolysis
Eur. Food Res. Technol.
243
1815-1828
2017
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 12046 (S4TJ23)
-
brenda
Stressler, T.; Eisele, T.; Ewert, J.; Kranz, B.; Fischer, L.
Proving the synergistic effect of Alcalase, PepX and PepN during casein hydrolysis by complete degradation of the released opioid precursor peptide VYPFPGPIPN
Eur. Food Res. Technol.
245
61-71
2019
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 12046 (S4TJ23)
-
brenda
De, A.; Lupidi, G.; Petrelli, D.; Vitali, L.
Molecular cloning and biochemical characterization of Xaa-Pro dipeptidyl-peptidase from Streptococcus mutans and its inhibition by anti-human DPP IV drugs
FEMS Microbiol. Lett.
363
fnw066
2016
Streptococcus mutans (Q8DVS2), Streptococcus mutans, Streptococcus mutans ATCC 700610 (Q8DVS2)
brenda
Giannoglou, M.; Alexandrakis, Z.; Stavros, P.; Katsaros, G.; Katapodis, P.; Nounesis, G.; Taoukis, P.
Effect of high pressure on structural modifications and enzymatic activity of a purified X-prolyl dipeptidyl aminopeptidase from Streptococcus thermophilus
Food Chem.
248
304-311
2018
Streptococcus thermophilus, Streptococcus thermophilus ACA-DC 0022
brenda
Miyabe, R.; Takahashi, Y.; Matsufuji, H.; Ogihara, J.; Ito, K.; Kawai, Y.; Masuda, T.; Suzuki, K.; Oda, M.
Purification and partial characterization of an X-prolyl-dipeptidyl aminopeptidase from lactobacillus gasseri me-284
Food Sci. Technol. Res.
21
445-451
2015
Lactobacillus gasseri, Lactobacillus gasseri ATCC 33323
-
brenda
Hafeez, Z.; Cakir-Kiefer, C.; Lecomte, X.; Miclo, L.; Dary-Mourot, A.
The X-prolyl dipeptidyl-peptidase PepX of Streptococcus thermophilus initially described as intracellular is also responsible for peptidase extracellular activity
J. Dairy Sci.
102
113-123
2019
Streptococcus thermophilus (Q03J44), Streptococcus thermophilus LMD-9 (Q03J44)
brenda
STressler, T.; Eisele, T.; Kranz, B.; Fischer, L.
PepX from Lactobacillus helveticus Automated multi-step purification and determination of kinetic parameters with original tripeptide substrates
J. Mol. Catal. B
108
103-110
2014
Lactobacillus helveticus (S4TJ23), Lactobacillus helveticus ATCC 12046 (S4TJ23)
-
brenda
Uestuen-Aytekin, O.e.; Arisoy, S.; Aytekin, A.O.e.; Yildiz, E.
Statistical optimization of cell disruption techniques for releasing intracellular X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis spp. lactis
Ultrason. Sonochem.
29
163-171
2016
Lactococcus lactis ssp. lactis, Lactococcus lactis ssp. lactis (A0A1V0NIQ5), Lactococcus lactis ssp. lactis NRRL B-1821, Lactococcus lactis ssp. lactis NRRL B-1821 (A0A1V0NIQ5)
brenda