Information on EC 3.4.24.14 - procollagen N-endopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.14
-
RECOMMENDED NAME
GeneOntology No.
procollagen N-endopeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-/-Gln and of alpha1(II) and alpha2(I) at Ala-/-Gln
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
68651-94-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ADAMTS2; gene ADAMTS2
UniProt
Manually annotated by BRENDA team
gene ADAMTS2; gene ADAMTS2
UniProt
Manually annotated by BRENDA team
gene ADAMTS2; gene ADAMTS2
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene ADAMTS2; gene ADAMTS2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
the N-propeptides of collagen are removed first, most probably in the Golgi or in the ERGIC (ER-Golgi intermediate compartment). In contrast, the C-propeptides are cleaved in a post-Golgi compartment
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pNcollagen
pCCollagen + oligopeptide
show the reaction diagram
pro-collagen + H2O
collagen + collagen N-propeptide
show the reaction diagram
procollagen I + H2O
?
show the reaction diagram
procollagen I + H2O
pCCollagen I + oligopeptide
show the reaction diagram
procollagen II + H2O
?
show the reaction diagram
procollagen II + H2O
pCCollagen II + oligopeptide
show the reaction diagram
procollagen III + H2O
pCCollagen III + oligopeptide
show the reaction diagram
-
removes the N-terminal propeptide from the native procollagen III, ADAMTS2 purified from skin is unable to process type III procollagen despite its activity on type I procollagen
-
-
?
procollagen V + H2O
pCCollagen V + oligopeptide
show the reaction diagram
-
processes the aminopropetide at the end of the variable domain, cleavage sequence is different from previously described sites for ADAMTS-2
-
-
?
type I procollagen + H2O
?
show the reaction diagram
-
-
-
-
?
type II procollagen + H2O
?
show the reaction diagram
-
-
-
-
?
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
pro-collagen + H2O
collagen + collagen N-propeptide
show the reaction diagram
procollagen I + H2O
?
show the reaction diagram
procollagen I + H2O
pCCollagen I + oligopeptide
show the reaction diagram
-
-
-
-
?
procollagen II + H2O
?
show the reaction diagram
type I procollagen + H2O
?
show the reaction diagram
-
-
-
-
?
type II procollagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-dipyridyl
2-mercaptoethanol
alpha2-Macroglobulin
-
-
-
ammonium persulfate
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94% inhibition at 10 micromol/ml
concanavalin A
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decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
dithiothreitol
Fe2+
-
-
ferrocene derivatives
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-
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Fetal bovine serum
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glutathione
-
-
heparan sulfate
heparin
metal chelator
-
potent inhibitor
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NaCl
-
40% inhibition at 0.3 M
p-hydroxymercuribenzoate
-
-
papilin
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Pb2+
-
-
phosphate
Poly-L-aspartate
Poly-L-glutamate
Reducing agent
-
potent inhibitor
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TIMP-3
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inhibits ADAMTS-2 in vitro in the presence of procollagen I and II, addition of heparin enhances the ability of TIMP-3 to inhibit the enzyme
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TIMP3
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Tris-HCl
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80% inhibition at 0.3 M
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dextran sulfate
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increases rate of cleavage about 4fold
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.0005
pNcollagen I
-
-
-
0.0028
pNcollagen, carboxymethylated
-
-
-
0.000035 - 0.435
procollagen I
-
0.000225
procollagen II
-
-
-
0.001
propeptide of collagen alpha-1 chain, propeptide of collagen alpha-2 chain
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-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.0967
procollagen I
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 0.602
TIMP-3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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procollagen I
7.4 - 9
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procollagen I
7.4
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procollagen I
7.5
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-
7.5 - 8
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procollagen
7.9 - 8.3
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procollagen I
8.3
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procollagen I
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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inactive below, procollagen I as substrate
6.6 - 8.8
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procollagen I as substrate, 50% of optimum activity at pH 6.6 and pH 8.8
6.7 - 9.5
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procollagen I as substrate, 45% of optimum activity at pH 6.7 and pH 9.5
6.8 - 9.5
-
procollagen I as substrate, 20% of optimum activity at pH 6.8 and pH 9.5
7 - 9.3
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procollagen I as substrate, more than 50% of optimum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36
-
procollagen I as substrate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
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inactive above, procollagen I as substrate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
enzyme expression; enzyme expression; enzyme expression
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
enzyme expression; enzyme expression; enzyme expression, overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids
Manually annotated by BRENDA team
overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
brefeldin A treatment of tendon explant cultures shows that N-proteinase activity is present in the resulting fused ER (endoplasmic reticulum)-Golgi compartment
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
gel filtration
107000
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chromatography
118000
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immunoprecipitation, truncated form
130000
-
gel filtration
132000
-
immunoprecipitation, full-length mature form
177000
-
immunoprecipitation, full size enzyme after removal of the signal peptide
320000
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gel filtration
500000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1* 107000, SDS-PAGE
oligomer
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SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
side-chain modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
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type I/II procollagen N-proteinase
37035
6.7 - 9.6
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-
37048
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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90% of activity recovered after 60 min
45
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90% of activity recovered after 30 min, 83% of activity recovered after 90 min
48
-
75% of activity recovered after 30 min
55
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10% of activity recovered after 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% loss of activity upon lyophilization
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Ca2+ stabilizes
stable to repeated thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, 2 days, stable
-
4 to -20°C, 0.05 M Tris-HCl, 0.75 M NaCl, 0.02% Brij 35, 0.01% NaN3, pH 7.5, 1-2 months, 90% activity recovered
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
400-6000fold purified by ammonium sulfate precipitation, concanavalin A and heparin-Sepharose chromatography and affinity chromatography
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from tendon; partially from skin
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partial
-
partially purified
-
purified 1000-16000fold to near homogeneity by different chromatographies
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ADAMTS14, alternative splicing is possible; gene ADAMTS2, alternative splicing is possible; gene ADAMTS3
gene ADAMTS14, alternative splicing is possible; gene ADAMTS2, sequence comparisons, alternative splicing is possible; gene ADAMTS3
gene ADAMTS2, sequence comparisons
gene ADAMTS2, sequence comparisons, alternative splicing is possible
recombinant bovine ADAMTS-2 is produced in HEK 293-EBNA cells
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recombinant expression in human tumor cell line HT-1080
subcloned in a pCDNA3 vector, expression in HT1080, W126, COS, Balb, MCF7, SaOS2 and 293EBNA cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme exxpression is upregulated by glucocorticoids
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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ADAMTS2 diplays procollagen III N-endopeptidase activity, proteolytic processing of ADAMTS2 may generate fragments displaying specifically either procollagen I/II or procollagen III N-endopeptidase acitvity