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
3.4.17.3
-
RECOMMENDED NAME
GeneOntology No.
lysine carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Release of a C-terminal basic amino acid, preferentially lysine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
P15169
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
activated thrombin-activable fibrinolysis inhibitor
-
-
anaphylatoxin inactivator
-
-
-
-
Arginine carboxypeptidase
-
-
-
-
bradykinase
-
-
-
-
bradykinin-decomposing enzyme
-
-
-
-
bradykininase
-
-
-
-
carboxypeptidase B
-
-
carboxypeptidase B
-
-
carboxypeptidase N
-
-
-
-
carboxypeptidase N
-
-
carboxypeptidase N
P15169
-
carboxypeptidase N
-
-
carboxypeptidase N
-
-
carboxypeptidase, arginine
-
-
-
-
CPase N
-
-
-
-
CPN
-
-
-
-
CPN
P15169
-
CPN
Q9JJN5
-
CPN1
-
-
creatine kinase conversion factor
-
-
-
-
creatinine kinase convertase
-
-
-
-
EC 3.4.12.7
-
-
formerly
-
hippuryllysine hydrolase
-
-
-
-
kininase I
-
-
-
-
kininase Ia
-
-
-
-
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
plasma carboxypeptidase
-
-
plasma carboxypeptidase
-
-
Plasma carboxypeptidase B
-
-
-
-
protaminase
-
-
-
-
SCPN
-
-
-
-
TAFIa
-
-
thrombin-activatable carboxypeptidase B
-
-
thrombin-activatable fibrinolysis inhibitor
-
-
thrombin-activatable procarboxypeptidase B
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-89-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
the enzyme exists in two forms: carboxypeptidase N1, and carboxypeptidase N2 which can be differentiated by their activities towards hippuryl-L-Arg and hippuryl-L-Lys
-
-
Manually annotated by BRENDA team
; carboxypeptidase N, small subunit
Swissprot
Manually annotated by BRENDA team
female and male C57BL/6 mice
-
-
Manually annotated by BRENDA team
enzyme form CN1 and CN2
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
ATCC 15909
-
-
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
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
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
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
-
i.e. bradykinin, removal of C-terminal Arg
-
-
?
benzoyl-Ala-Arg + H2O
benzoyl-Ala + 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-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-Arg + H2O
benzoyl-Gly + Arg
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-argininic acid + H2O
benzoyl-Gly + argininic acid
show the reaction diagram
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
show the reaction diagram
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
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
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
P15169
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
inactivates bradykinin
-
-
-
C3a69-77 + H2O
?
show the reaction diagram
P15169
-, peptide derived from bradykinin
-
-
?
C5a66-74 + H2O
?
show the reaction diagram
P15169
-, peptide derived from bradykinin
-
-
?
chemerin + H2O
?
show the reaction diagram
P15169
-, CPB enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine, CPN enhances the bioactivity of 10-mer chemerin peptide NH2-YFPGQFAFSK-COOH by removing the carboxyl-terminal lysine
-
-
?
fibrinopeptide A + H2O
Arg + ?
show the reaction diagram
-
very low activity
-
?
fibrinopeptide alphaArg96-104 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide B + H2O
Arg + ?
show the reaction diagram
-
-
-
?
fibrinopeptide betaLys125-133 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide gammaLys54-62 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide gammaLys77-85 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide-alpha-Arg96-104 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide-beta-Lys125-133 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide-gamma-Lys54-62 + H2O
?
show the reaction diagram
P15169
-
-
-
?
fibrinopeptide-gamma-Lys77-85 + H2O
?
show the reaction diagram
P15169
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
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-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
show the reaction diagram
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-L-Lys + H2O
furylacryloylalanine-Ala + Lys
show the reaction diagram
-
low reaction rate
-
?
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-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-, Q9JJN5
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
show the reaction diagram
-, Q9JJN5
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-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 + H2O
Hippuric acid + L-Lys
show the reaction diagram
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
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
-
?
kallikrein + H2O
?
show the reaction diagram
-
plasma or urinary
-
-
?
kinin + H2O
?
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
-
-
-
-
?
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
P15169
sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities, sequential cleavages of either a prochemerin peptide or recombinant full-length prochemerin by plasmin and CPN/CPB substantially increases their chemotactic activities. Endogenous CPN present in circulating plasma enhances the activity of plasmin-cleaved prochemerin
-
-
?
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
P15169
bioacivity of 10-mer chemerin peptide, chemerin 149-158, is enhanced by removing the carboxyl-terminal lysine
-
-
?
YFPGQFAFSKALPRS + H2O
?
show the reaction diagram
P15169
sequential cleavage of prochemerin peptide, chemerin 149-163, by CPB increases chemotactic activities
-
-
?
Leu-Trp-Met-Arg + H2O
Leu-Trp-Met + Arg
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme cleaves C-terminal Lys faster than Arg in most substrates
-
-
-
additional information
?
-
-, Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
-, Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation, C-terminal cleavage of stromal cell-derived factor-1alpha reducing the substrate's biological activity, SDF-1alpha
-
-
-
additional information
?
-
-
the enzyme releases C-terminal Arg and Lys from peptide substrates, such as bradykinin, kallidin, or Met-Lys-bradykinin
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
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
Bradykinin + H2O
?
show the reaction diagram
-
inactivates bradykinin
-
-
-
additional information
?
-
-, Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
-
-
additional information
?
-
-, Q9JJN5
carboxypeptidase N is not an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme is involved in regulation of inflammation, overview, the enzyme acts as anaphylatoxin inactivator
-
-
-
additional information
?
-
-
the enzyme is responsible for regulatory C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation
-
-
-
additional information
?
-
-
activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested fibrin clot
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can replace Co2+ as cofactor
Zinc
-
Zn2+ required
Zinc
-
zinc metalloenzyme
Zinc
-
contains 0.96 gatom of zinc per mol of enzyme; zinc metalloenzyme
Zinc
-
zinc metalloprotease
Zn2+
-
zinc-metalloprotease
Co2+
-
activates
additional information
-
metalloenzyme, methyl is tightly bound to the apoenzyme at neutral pH
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
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
-
-
6-Aminohexanoic acid
-
with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
6-Aminohexanoic acid
-
-
Arg
-
D-Arg; L-Arg; with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
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
-
-
benzoyl-L-Arg
-
with benzoyl-Gly-Arg as substrate
Benzyloxycarbonyl-Arg
-
with benzoyl-Gly-Arg as substrate
beta-Ala
-
weak
bromoacetyl-D-Arg
-
irreversible
Captopril
-
-
DL-2-mercaptomethyl-3 guanidinoethylthiopropanoic acid
P15169
specific inhibitor for CPN but not CPB
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00593 mM
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.0128 mM
Guanidinoethylmercaptosuccinic acid
-
weak
Guanidinoethylmercaptosuccinic acid
-
-
guanidinopropylsuccinic acid
-
weak
hippuric acid
-
with benzoyl-Gly-Arg as substrate
Hippuryl-L-argininic acid
-
with benzoyl-Gly-Arg as substrate
Histargin
-
and analogs
Lisinopril
-
-
Lys
-
with hippuryl-argininic acid as substrate
Nalpha-acetyl-Arg
-
with benzoyl-Gly-Lys or benzoyl-Gly-Arg as substrate
Nalpha-acetyl-Lys
-
with benzoyl-Gly-Lys as substrate
Peptide fragments of bradykinin
-
-
-
phosphormaidon
-
-
Potato carboxypeptidase inhibitor
Q9JJN5
-
-
protamine
-
-
additional information
-
no inhibition by CKPAKNARC, i.e. CPI-2KR
-
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thrombin-thrombomodulin complex
P15169
on the vascular endothelial surface
-
thrombin-thrombomodulin complex
-
on the vascular endothelial surface
-
additional information
-
the enzyme expression level is unaffected by lipopolysaccharides
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.28
-
benzoyl-Ala-Arg
-
-
0.25
-
Benzoyl-Ala-Lys
-
-
0.35
-
Benzoyl-Ala-Lys
-
-
0.1
-
benzoyl-Gly-Arg
-
-
6.7
-
benzoyl-Gly-Arg
-
-
1.4
-
Benzoyl-Gly-Lys
-
-
6.3
-
Benzoyl-Gly-Lys
-
-
0.0004
-
bradykinin
-
-
0.0706
-
bradykinin
P15169
-
0.302
-
bradykinin
P15169
-
0.706
-
bradykinin
P15169
-
0.035
-
C3a69-77
P15169
peptide derived from bradykinin
0.0359
-
C3a69-77
P15169
-
0.077
-
C3a69-77
P15169
peptide derived from bradykinin
0.219
-
C5a66-74
P15169
peptide derived from bradykinin
0.602
-
C5a66-74
P15169
peptide derived from bradykinin
0.1228
-
chemerin
P15169
;
-
0.17
-
chemerin
P15169
-
-
0.13
-
des-Arg9-bradykinin
-
-
0.361
-
fibrinopeptide alphaArg96-104
P15169
-
-
0.448
-
fibrinopeptide alphaArg96-104
P15169
-
-
0.0532
-
fibrinopeptide betaLys125-133
P15169
-
-
0.143
-
fibrinopeptide betaLys125-133
P15169
-
-
0.34
-
fibrinopeptide gammaLys54-62
P15169
-
-
0.657
-
fibrinopeptide gammaLys54-62
P15169
-
-
0.238
-
fibrinopeptide gammaLys77-85
P15169
-
-
3.727
-
fibrinopeptide gammaLys77-85
P15169
-
-
0.3614
-
fibrinopeptide-alpha-Arg96-104
P15169
-
-
0.0143
-
fibrinopeptide-beta-Lys125-133
P15169
-
-
0.034
-
fibrinopeptide-gamma-Lys54-62
P15169
-
-
0.2389
-
fibrinopeptide-gamma-Lys77-85
P15169
-
-
0.26
-
furylacryloyl-Ala-Arg
-
-
0.34
-
furylacryloyl-Ala-Lys
-
-
0.3
-
furylacryloylalanyl-L-Lys
-
-
0.14
-
hippuryl-Arg
-
-
1.8
-
hippuryl-Arg
-
-
1.2
-
hippuryl-L-Arg
-
-
6.93
-
hippuryl-L-Arg
-
-
0.3
-
Hippuryl-L-argininic acid
-
-
3.3
-
Hippuryl-L-Lys
-
-
35.8
-
Hippuryl-L-Lys
-
-
5.9
-
Leu-Trp-Met-Arg
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
139
-
benzoyl-Ala-Arg
-
-
352
-
Benzoyl-Ala-Lys
-
-
9.1
-
bradykinin
P15169
-
19.7
-
bradykinin
P15169
;
8.4
-
C3a69-77
P15169
; peptide derived from bradykinin
57.9
-
C3a69-77
P15169
peptide derived from bradykinin
9.3
-
C5a66-74
P15169
peptide derived from bradykinin
29.5
-
C5a66-74
P15169
peptide derived from bradykinin
2.7
-
chemerin
P15169
;
-
80.35
-
chemerin
P15169
-
-
1.5
-
fibrinopeptide alphaArg96-104
P15169
-
-
2.9
-
fibrinopeptide alphaArg96-104
P15169
-
-
13.6
-
fibrinopeptide betaLys125-133
P15169
-
-
109.1
-
fibrinopeptide betaLys125-133
P15169
-
-
2.6
-
fibrinopeptide gammaLys54-62
P15169
-
-
3.5
-
fibrinopeptide gammaLys54-62
P15169
-
-
5.9
-
fibrinopeptide gammaLys77-85
P15169
-
-
11.8
-
fibrinopeptide gammaLys77-85
P15169
-
-
1.5
-
fibrinopeptide-alpha-Arg96-104
P15169
-
-
13.6
-
fibrinopeptide-beta-Lys125-133
P15169
-
-
2.6
-
fibrinopeptide-gamma-Lys54-62
P15169
-
-
5.9
-
fibrinopeptide-gamma-Lys77-85
P15169
-
-
31
-
furylacryloyl-Ala-Arg
-
-
97
-
furylacryloyl-Ala-Lys
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00593
-
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00593 mM
0.0128
-
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.0128 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0225
-
-
-
55.3
-
-
-
104
-
-
-
105.3
-
-
purified native enzyme
additional information
-
-
assay
additional information
-
-
-
additional information
-
-
spectrophotometric assay
additional information
-
-
-
additional information
-
-
assay
additional information
-
-
comparison of serum and plasma enzyme activities using substrate stromal cell-derived factor-1alpha
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
-
7.2
-
-
assay at
8.7
-
-
hippuryl-L-Arg
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
pH 5.5: about 65% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
P15169
activity assay; assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
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
-
cortex and medulla
Manually annotated by BRENDA team
-
plasma membrane and fibroblasts
Manually annotated by BRENDA team
-
microvilli
Manually annotated by BRENDA team
-
benign hypertrophy
Manually annotated by BRENDA team
Q9JJN5
weak expression
Manually annotated by BRENDA team
additional information
-
constitutive expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
gel filtration
315000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 49000 + x * 55000 + x * 83000, SDS-PAGE
?
-
x * 45000 + x * 90000, SDS-PAGE
?
-
x * 48000 + x * 81000-87000, SDS-PAGE
?
-
x * 30000 + x * 50000 + x * 90000, SDS-PAGE
tetramer
-
2 * 49000-55000 + 2 * 83000-98000.
tetramer
-
2 * 83000 + 2 * 50000, the two high molecular weight subunits, 58762 Da determined by calculation from nucleotide sequence, protect the two 50000 Da subunits, and keep them into circulation
tetramer
-
2 * 48000 + 2 * 83000, the 48000 Da subunit is as active as the intact enzyme, the 83000 Da subunit is inactive but stabilizes the 48000 Da subunit, SDS-PAGE
dimer
-
2 * 52000, the homodimeric enzyme consists of two small subunits
additional information
-
subunit interaction
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
presence of significant amounts of glucosamine, mannose, galactose, fucose, sialic acid; the carbohydrate is primarily attached to the larger subunit, representing 28% of its weight. Two forms detected in isoelectric focusing with pI of 3.8 and 4.3. The difference is attributed to differences in sialic acid content of the two forms
side-chain modification
-
carbohydrate accounts for 17% of the weight, contains significant amounts; presence of significant amounts of glucosamine, mannose, galactose, fucose, sialic acid
side-chain modification
-
the enzyme contains seven potential N-linked glycosylation sites and a threonine/serine-rich region which is a potential site for attachment of O-linked carbohydrate
side-chain modification
-
the 83000 Da subunit contains carbohydrate
side-chain modification
-
the subunit of MW 81000-87000 Da contains carbohydrate
side-chain modification
-
sialoprotein with at least two forms, differing in sialic acid content. Sialic acid may possibly influence stability
side-chain modification
-
the 83000 Da subunit contains about 27% carbohydrate per weight, it may contain both N-linked and O-linked carbohydrate
side-chain modification
-
the 90000 Da subunit contains carbohydrate, no carbohydrate is detected in the subunits of MW 50000 Da and 30000 Da
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
37
-
-
2 h, stable
37
-
-
no loss of activity for up to 25 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
4°C, stable for at least 3 months
-
4°C, stable for 20 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
from serum 175.5fold by ammonium sulfate fractionation, anion exchange chromatography and lysine affinity chromatography to homogeneity
-
partial
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning of the small active subunit
-
gene structure comparison, DNA and amino acid sequence determination and analysis
-
expression in COS-7 cells
Q9JJN5
gene structure comparison, DNA and amino acid sequence determination and analysis
-
expression in CHO cells
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
data support the thesis that thrombin-activable CPB has broad anti-inflammatory properties