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Information on EC 3.4.14.11 - Xaa-Pro dipeptidyl-peptidase and Organism(s) Lactococcus lactis and UniProt Accession P22346

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Lactococcus lactis
UNIPROT: P22346 not found.
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The taxonomic range for the selected organisms is: Lactococcus lactis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pepxp, x-prolyl dipeptidyl peptidase, prolyl dipeptidyl aminopeptidase, xaa-pro dipeptidyl-peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PepX
-
-
-
-
X-PDAP
-
-
-
-
X-Pro dipeptidyl-peptidase
-
-
-
-
X-prolyl dipeptidyl aminopeptidase
-
-
-
-
X-prolyl dipeptidyl peptidase
X-prolyl-dipeptidyl aminopeptidase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
54249-88-6
not distinguishable from EC 3.4.14.5 in Chemical Abstracts
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
show the reaction diagram
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
show the reaction diagram
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
?
beta-casomorphin + H2O
?
show the reaction diagram
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Ala-7-amido-4-methylcoumarin + H2O
Gly-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
show the reaction diagram
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly-Pro + Ala
show the reaction diagram
-
-
-
-
?
Gly-Pro-Gly-Gly + H2O
Gly-Pro + Gly-Gly
show the reaction diagram
-
-
-
-
?
His-Pro-Leu + H2O
His-Pro + Leu
show the reaction diagram
-
-
-
-
?
His-Pro-Tyr + H2O
His-Pro + Tyr
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
Leu-Ala-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Ala-Val-Pro-Tyr-Pro-Gln + H2O
?
show the reaction diagram
-
fragment 176-182 of beta-casein
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
show the reaction diagram
-
85% of the activity with Arg-Pro-p-nitroanilide
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
show the reaction diagram
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metal-independent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Diprotin A
IC50: 0.26 mM
Diprotin B
IC50: 0.6 mM
Val-pyrrolidide
IC50: 0.03 mM
1,10-phenanthroline
-
-
diisopropylfluorophosphate
-
-
EDTA
-
no inhibition
iodoacetate
-
-
Phenylmethanesulphonyl fluoride
-
0.1 mM, 20 min at 40°C, 40% loss of activity. 1 mM, complete inhibition after 20 min
phenylmethylsulfonyl fluoride
-
-
Urea
-
2.0 M
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
-
up to 25%, enhances activity
Triglyme
-
up to 25%, enhances activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.92
Arg-Pro-p-nitroanilide
-
-
0.0457
Glu-Pro-7-amido-4-methylcoumarin
-
-
0.385
Gly-Ala 4-methylcoumarin 7-amide
-
-
0.107
Gly-Pro 4-nitroanilide
-
-
0.0141
Gly-Pro-7-amido-4-methylcoumarin
-
-
0.0092
Leu-Pro-7-amido-4-methylcoumarin
-
-
0.231
Lys-Ala-7-amido-4-methylcoumarin
-
-
0.0146
Lys-Pro-7-amido-4-methylcoumarin
-
-
0.0124
Phe-Pro-7-amido-4-methylcoumarin
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
181
Arg-Pro 4-nitroanilide
-
-
62.9
Glu-Pro-7-amido-4-methylcoumarin
-
-
2.1
Gly-Ala-7-amido-4-methylcoumarin
-
-
178
Gly-Pro 4-nitroanilide
-
-
62.1 - 69.8
Gly-Pro-7-amido-4-methylcoumarin
2180
Gly-Pro-Ala
-
-
46.4
Gly-Pro-Gly-Gly
-
-
418
His-Pro-Leu
-
-
670
His-Pro-Tyr
-
-
26
L-Ala-L-Ala-7-amido-4-methylcoumarin
-
-
-
120
Leu-Ala-Pro
-
-
43.4
Leu-Pro-7-amido-4-methylcoumarin
-
-
17.1
Lys-Ala-7-amido-4-methylcoumarin
-
-
61.6
Lys-Pro-7-amido-4-methylcoumarin
-
-
78.4
Phe-Pro-7-amido-4-methylcoumarin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
Diprotin A
Lactococcus lactis
IC50: 0.26 mM
0.6
Diprotin B
Lactococcus lactis
IC50: 0.6 mM
0.03
Val-pyrrolidide
Lactococcus lactis
IC50: 0.03 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
little variation in activity in this range
7
-
substrate: Arg-Pro-p-nitroanilide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
pH 5.0: 88% of maximal activity, pH 7.0: maximal activity
5.5 - 8.5
-
pH 5.5: 50% of maximal activity, pH 8.5: activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
50% of maximal activity at 30°C, maximum at 40-50°C
40 - 50
-
40°C: 95% of maximal activity, 50°C: 98% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the C-terminal moiety probably plays a role in tropism of the enzyme towards the cellular membrane
Manually annotated by BRENDA team
-
loosely bound
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
gel filtration
160000 - 180000
-
gel filtration
190000
-
gel filtration
82000
-
x * 82000, SDS-PAGE
85000
-
2 * 85000, SDS-PAGE with or without 2-mercaptoethanol
90000
-
2 * 90000, SDS-PAGE
additional information
-
identification of the active site serine
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 82000, SDS-PAGE
dimer
additional information
each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
1 h, 40% loss of activity
4
-
1 h, 20% loss of activity
additional information
-
glycerol, triglyme and DMSO, up to 25% increase stability at 4°C and at 30°C. Methanol, isopropanol, N,N-dimethylformamide and acetone increase stability at 4°C and allow a limited stability at 30°C. Ethanol, dioxane and acetonitrile allow a limited stability at 4°C and no stability at 30°C
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
increases stability at 4°C and allow a limited stability at 30°C
acetonitrile
-
allows a limited stability at 4°C and no stability at 30°C
dioxane
-
allows a limited stability at 4°C and no stability at 30°C
DMSO
-
up to 25% increase stability at 4°C and at 30°C
Ethanol
-
allows a limited stability at 4°C and no stability at 30°C
Glycerol
-
up to 25% increase stability at 4°C and at 30°C
N,N-dimethylformamide
-
increases stability at 4°C and allow a limited stability at 30°C
triglyme
-
up to 25% increase stability at 4°C and at 30°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 60% glycerol, stable for 30 days
-
4°C, 20 mM Tris buffer, 20% loss of activity after 1 h
-
4°C, pH 8.0, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low PepXP activity is a predictor for subspecies Lactococcus lactis lactis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team