Information on EC 3.4.17.3 - lysine carboxypeptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.17.3
-
RECOMMENDED NAME
GeneOntology No.
lysine carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of a C-terminal basic amino acid, preferentially lysine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
9013-89-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC 15909
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Phe-Ser-Pro-Phe-Arg + H2O
acetyl-Phe-Ser-Pro-Phe + Arg
show the reaction diagram
-
-
-
-
?
activated complement C3a + H2O
?
show the reaction diagram
-
-
-
-
?
activated complement C5a + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
show the reaction diagram
-
reaction is less efficient than reaction with EC 3.4.17.20
-
?
anaphylatoxin + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
show the reaction diagram
benzoyl-Ala-Arg + H2O
benzoyl-Ala + Arg
show the reaction diagram
benzoyl-Ala-Lys + H2O
?
show the reaction diagram
benzoyl-argininic acid + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
show the reaction diagram
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
show the reaction diagram
benzyloxycarbonyl-Ala-Arg + H2O
benzyloxycarbonyl-Ala + Arg
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
Lys + benzyloxycarbonyl-Val-Gly-Lys
show the reaction diagram
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
C3a69-77 + H2O
?
show the reaction diagram
C5a66-74 + H2O
?
show the reaction diagram
chemerin + H2O
?
show the reaction diagram
dansyl-Phe-Ala-Arg + H2O
dansyl-Phe-Ala + L-arginine
show the reaction diagram
-
-
-
-
?
fibrinopeptide A + H2O
Arg + ?
show the reaction diagram
-
very low activity
-
?
fibrinopeptide alphaArg96-104 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide B + H2O
Arg + ?
show the reaction diagram
-
-
-
?
fibrinopeptide betaLys125-133 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide gammaLys54-62 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide gammaLys77-85 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide-alpha-Arg96-104 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide-beta-Lys125-133 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide-gamma-Lys54-62 + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide-gamma-Lys77-85 + H2O
?
show the reaction diagram
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
show the reaction diagram
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
show the reaction diagram
furylacryloyl-Gly-Arg + H2O
furylacryloyl-Gly + Arg
show the reaction diagram
-
-
-
-
?
furylacryloyl-Gly-Lys + H2O
furylacryloyl-Gly + Lys
show the reaction diagram
-
-
-
-
?
Gly-His-Lys + H2O
Gly-His + Lys
show the reaction diagram
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
Hippuryl-L-argininic acid + H2O
Hippuric acid + argininic acid
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuryl-L-His + L-Leu
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
show the reaction diagram
hippuryl-L-Lys-L-Leu + H2O
hippuryl-L-Lys + L-Leu
show the reaction diagram
-
-
-
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
show the reaction diagram
-
i.e. C5a, reaction is less efficient than reaction with EC 3.4.17.20
-
?
His-tagged C3f peptide + H2O
?
show the reaction diagram
-
CPN cleaves the C-terminal Arg of C3f_R1310-R1320 to produce C3f_R1310-L1319
-
-
?
kallikrein + H2O
?
show the reaction diagram
-
plasma or urinary
-
-
?
kinin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Trp-Met-Arg + H2O
Leu-Trp-Met + Arg
show the reaction diagram
-
-
-
?
Phe-Ser-Pro-Phe-Arg + H2O
Phe-Ser-Pro-Phe + Arg
show the reaction diagram
-
-
-
-
?
plasmin + H2O
?
show the reaction diagram
-
-
-
-
-
polylysine + H2O
Lys
show the reaction diagram
Pro-Gly-Lys-Ala-Arg + H2O
Pro-Gly-Lys-Ala + Arg
show the reaction diagram
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro-Phe-Gly + Lys
show the reaction diagram
-
-
-
?
Pro-Phe-Lys + H2O
Pro-Phe + Lys
show the reaction diagram
-
-
-
-
?
Pro-Phe-Lys-Gly + H2O
Pro-Phe-Lys + Gly
show the reaction diagram
-
-
-
-
?
prochemerin + H2O
?
show the reaction diagram
salmine + H2O
Arg + ?
show the reaction diagram
-
-
-
?
Thr-Pro-Arg-Lys + H2O
Thr-Pro-Arg + Lys
show the reaction diagram
-
-
-
?
thrombin-cleaved osteopontin + H2O
?
show the reaction diagram
-
-
-
-
?
trypsin + H2O
?
show the reaction diagram
-
-
-
-
-
YFPGQFAFSK + H2O
YFPGQFAFS + lysine
show the reaction diagram
bioacivity of 10-mer chemerin peptide, chemerin 149-158, is enhanced by removing the carboxyl-terminal lysine
-
-
?
YFPGQFAFSKALPRS + H2O
?
show the reaction diagram
sequential cleavage of prochemerin peptide, chemerin 149-163, by CPB increases chemotactic activities
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bradykinin + H2O
?
show the reaction diagram
-
inactivates bradykinin
-
-
-
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metalloenzyme, methyl is tightly bound to the apoenzyme at neutral pH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,3-dimercatopropan-1-ol
-
-
2-mercaptoethanol
-
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
4-aminomethyl-cyclohexane carboxylic acid
-
with benzoyl-Gly-Lys as substrate
5-amino-n-pentanoic acid
-
-
-
6-Aminohexanoic acid
Argininic acid
-
inhibition of peptidase activity and esterase activity; with benzoyl-Gly-Lys, hippuryl-argininic acid or with benzoyl-Gly-Arg as substrate
benzoyl-L-Arg
Benzyloxycarbonyl-Arg
-
with benzoyl-Gly-Arg as substrate
beta-Ala
-
weak
bromoacetyl-D-Arg
-
irreversible
captopril
-
-
CoCl2
-
-
Cu2+
-
-
DL-2-mercaptomethyl-3 guanidinoethylthiopropanoic acid
specific inhibitor for CPN but not CPB
EF6265
Guanidinoethylmercaptosuccinic acid
guanidinopropylsuccinic acid
-
weak
hippuric acid
-
with benzoyl-Gly-Arg as substrate
Hippuryl-L-argininic acid
-
with benzoyl-Gly-Arg as substrate
His
-
weak
Histargin
-
and analogs
Lisinopril
-
-
MnCl2
-
-
Nalpha-acetyl-Arg
-
with benzoyl-Gly-Lys or benzoyl-Gly-Arg as substrate
Nalpha-acetyl-Lys
-
with benzoyl-Gly-Lys as substrate
NiSO4
-
-
Orn
-
weak
Peptide fragments of bradykinin
-
-
-
phosphormaidon
-
-
Potato carboxypeptidase inhibitor
-
-
protamine
-
-
Zn2+
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thrombin-thrombomodulin complex
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
benzoyl-Ala-Arg
-
-
0.25 - 0.35
Benzoyl-Ala-Lys
0.1 - 6.7
benzoyl-Gly-Arg
1.4 - 6.3
Benzoyl-Gly-Lys
0.0004 - 0.706
bradykinin
0.035 - 0.077
C3a69-77
0.219 - 0.602
C5a66-74
0.1228 - 0.17
chemerin
0.13
des-Arg9-bradykinin
-
-
0.361 - 0.448
fibrinopeptide alphaArg96-104
0.0532 - 0.143
fibrinopeptide betaLys125-133
0.34 - 0.657
fibrinopeptide gammaLys54-62
0.238 - 3.727
fibrinopeptide gammaLys77-85
0.3614
fibrinopeptide-alpha-Arg96-104
-
-
0.0143
fibrinopeptide-beta-Lys125-133
-
-
0.034
fibrinopeptide-gamma-Lys54-62
-
-
0.2389
fibrinopeptide-gamma-Lys77-85
-
-
0.26
furylacryloyl-Ala-Arg
-
-
0.34
furylacryloyl-Ala-Lys
-
-
0.3
furylacryloylalanyl-L-Lys
-
-
0.14 - 1.8
hippuryl-Arg
1.2 - 6.93
hippuryl-L-Arg
0.3
Hippuryl-L-argininic acid
-
-
3.3 - 35.8
Hippuryl-L-Lys
5.9
Leu-Trp-Met-Arg
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
139
benzoyl-Ala-Arg
Homo sapiens
-
-
352
Benzoyl-Ala-Lys
Homo sapiens
-
-
9.1 - 19.7
bradykinin
8.4 - 57.9
C3a69-77
9.3 - 29.5
C5a66-74
2.7 - 80.35
chemerin
1.5 - 2.9
fibrinopeptide alphaArg96-104
13.6 - 109.1
fibrinopeptide betaLys125-133
2.6 - 3.5
fibrinopeptide gammaLys54-62
5.9 - 11.8
fibrinopeptide gammaLys77-85
1.5
fibrinopeptide-alpha-Arg96-104
Homo sapiens
P15169
-
-
13.6
fibrinopeptide-beta-Lys125-133
Homo sapiens
P15169
-
-
2.6
fibrinopeptide-gamma-Lys54-62
Homo sapiens
P15169
-
-
5.9
fibrinopeptide-gamma-Lys77-85
Homo sapiens
P15169
-
-
31
furylacryloyl-Ala-Arg
Homo sapiens
-
-
97
furylacryloyl-Ala-Lys
Homo sapiens
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00593 - 0.0128
EF6265
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0225
-
-
55.3
-
-
105.3
-
purified native enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
assay at
7 - 7.5
-
-
8.7
-
hippuryl-L-Arg
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
pH 5.5: about 65% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
Manually annotated by BRENDA team
-
sigmoid part of colon
Manually annotated by BRENDA team
-
developmental expression of the enzyme small subunit CPN1, CPN1 expression proceeds the expression of the third complement component C3 by several days, RNA in situ hybridization
Manually annotated by BRENDA team
-
foreskin
Manually annotated by BRENDA team
-
fetal
Manually annotated by BRENDA team
-
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
Manually annotated by BRENDA team
-
metastatic
Manually annotated by BRENDA team
-
microvilli
Manually annotated by BRENDA team
-
benign hypertrophy
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
constitutive expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
gel filtration
122000
-
gel filtration
150000 - 160000
-
ultracentrifugal analysis, a second molecular weight species of 300000-320000 Da is detected
270000 - 280000
-
-
280000
-
gel filtration
300000 - 320000
-
ultracentrifugal analysis, a second molecular weight species of 150000-160000 Da is detected
315000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
room temperature, pH 4-5, 1 h, the 48000 Da subunit loses 94% of its activity, the intact enzyme loses 9% of its activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme, 4°C, pH 7,0, stable for 2 months
-
plasmin and trypsin cleave the enzyme to lower molecular weight fragments
-
SDS, 3 mM, 10 min, 55% loss of activity
-
the enzyme is stable in blood plasma for up to seven days after blood collection
-
urea, 4 M, complete inactivation in 10 min
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for 20 days
-
4°C, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from serum 175.5fold by ammonium sulfate fractionation, anion exchange chromatography and lysine affinity chromatography to homogeneity
-
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the small active subunit
-
expression in CHO cells
-
expression in COS-7 cells
gene structure comparison, DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
higher expression is detected in in short-day (SD; 8 : 16 h light/dark) acclimatised hamsters
-
the amount of CPN is increased in tumor tissues compared to that seen in normal breast tissue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
data support the thesis that thrombin-activable CPB has broad anti-inflammatory properties