We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.4.21.32 - brachyurin for references in articles please use BRENDA:EC3.4.21.32Word Map on EC 3.4.21.32
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of peptide bond
-
-
endopeptidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aspergillopeptidase C
-
-
-
-
clostridiopeptidase A
-
-
-
-
clostridiopeptidase I
-
-
-
-
clostridiopeptidase II
-
-
-
-
collagen peptidase
-
-
-
-
collagenase MMP-1
-
-
-
-
collagenolytic protease
-
-
-
-
collagenolytic serine protease
matrix metalloproteinase-1
-
-
-
-
matrix metalloproteinase-18
-
-
-
-
Matrix metalloproteinase-8
-
-
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
non-clip domain serine protease
-
peptidase, clostridio-, A
-
-
-
-
proteinase, Clostridium histolyticum, A
-
-
-
-
uca pugilator collagenolytic proteinase
-
-
-
-
collagenolytic serine protease
-
collagenolytic serine protease
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9001-01-8
not distinguished from EC 3.4.21.34, EC 3.4.21.35
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
greenshore crab
-
-
brenda
collected from the Xinxiang aquatic product market from September to October 2012 in Xinxiang, China
UniProt
brenda
atlantic cod
-
-
brenda
-
-
-
brenda
Novoden modestrus
-
-
-
brenda
-
-
-
brenda
shrimp
-
-
brenda
-
-
-
brenda
fiddler crab
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
active enzyme variaant PtSP
UniProt
brenda
inactive variant PtSPH1
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
absence of Ser catalytic residue results in the loss of serine protease activity of PtSPH1
physiological function
possible role of the enzyme in the invertebrate innate immune system
additional information
the enzyme contains a serine protease domain at the C-terminus; the enzyme contains a serine protease domain at the C-terminus
additional information
the enzyme contains a serine protease domain at the C-terminus; the enzyme contains a serine protease domain at the C-terminus
additional information
-
the enzyme contains a conserved catalytic triad of His, Asp, and Ser residues
additional information
the enzyme contains a conserved catalytic triad of His, Asp, and Ser residues
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Collagen + H2O
Hydrolyzed collagen
N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Arg-p-nitroanilide + H2O
?
N-benzoyl-L-Tyr ethyl ester + H2O
?
N-benzoyl-L-Tyr-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide + H2O
?
Nalpha-tosyl-L-Arg methyl ester + H2O
?
-
-
-
-
?
succinyl-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide + H2O
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
?
additional information
?
-
-
substrate succinyl-Ala-Ala-Pro-Xaa-p-nitroanilide for testing substrate specificity
-
-
-
Collagen + H2O
Hydrolyzed collagen
-
type I and III
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
type I,III, IV and V
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
type I
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
cleaves bovine collagen I chain C-terminal to Gln and Arg residues adjacent to the metallocollagenase site
-
-
?
Collagen + H2O
Hydrolyzed collagen
Novoden modestrus
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
calf skin collagen type III and bovine lens capsule collagen type IV
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
collagen type I
-
-
?
N-benzoyl-L-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
?
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
?
-
-
-
-
?
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ba2+
Novoden modestrus
-
0.06 mM, activation to 119% of control
Ca2+
Novoden modestrus
-
0.06 mM, activation to 135% of control
K+
Novoden modestrus
-
0.06 mM, activation to 123% of control
Li+
Novoden modestrus
-
0.06 mM, activation to 111% of control
Mg2+
-
activates
Mg2+
Novoden modestrus
-
0.06 mM, activation to 111% of control
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3,4-dichloro-isocoumarin
-
-
alpha1 protease inhibitor
-
-
-
basic pancreatic trypsin inhibitor
-
-
-
Cd2+
Novoden modestrus
-
0.06 mM, 29% inhibition
chicken ovoinhibitor
-
-
-
Cu2+
Novoden modestrus
-
0.06 mM, 26% inhibition
diisopropylfluorophosphate
EDTA
Novoden modestrus
-
0.2 mM, 46% inhibition. 0.5 mM, 95% inhibition
His
Novoden modestrus
-
0.2 mM, 51% inhibition. 0.7 nmM, 93% inhibition
Mn2+
Novoden modestrus
-
0.06 mM, 14% inhibition
Ni2+
Novoden modestrus
-
0.06 mM, 30% inhibition
Phenylmethylsulfonylfluoride
Soybean trypsin inhibitor
-
tosyl-L-Leu-chloromethylketone
Novoden modestrus
-
0.2 mM, complete inhibition
tosyl-Phe-CH2Cl
-
protease C
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
Novoden modestrus
-
0.2 mM, complete inhibition
diisopropylfluorophosphate
-
-
Hg2+
-
-
Hg2+
Novoden modestrus
-
0.06 mM, 19% inhibition
Phenylmethylsulfonylfluoride
-
-
Phenylmethylsulfonylfluoride
-
-
Phenylmethylsulfonylfluoride
-
-
Phenylmethylsulfonylfluoride
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
Novoden modestrus
-
0.2 mM, complete inhibition
-
Soybean trypsin inhibitor
-
-
-
tosyl-Lys-CH2Cl
-
-
tosyl-Lys-CH2Cl
-
protease A
Zn2+
-
-
Zn2+
Novoden modestrus
-
0.06 mM, 36% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.044
N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide
-
-
0.1
N-benzoyl-L-Arg-p-nitroanilide
-
-
1.11
N-benzoyl-L-Tyr ethyl ester
-
-
0.263
N-benzoyl-L-Tyr-p-nitroanilide
-
-
0.12
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide
-
-
0.233
Nalpha-tosyl-L-Arg methyl ester
-
-
0.14
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide
-
-
0.09
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10550
Novoden modestrus
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 8
Novoden modestrus
-
hydrolysis of collagen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.5 - 8.5
Novoden modestrus
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 50% of maximal activity, hydrolysis of collagen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
55
Novoden modestrus
-
hydrolysis of collagen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
45 - 60
Novoden modestrus
-
45°C: about 40% of maximal activity, 60°C: about 45% of maximal activity, hydrolysis of collagen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3
calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
;
brenda
-
brenda
;
brenda
-
brenda
low expression level
brenda
-
brenda
; very high expression level
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
the PtSPH1 transcript is mainly expressed in stomach
brenda
additional information
-
the enzyme expression is tissue-related with the highest expression in hemocytes and widely distributed
brenda
additional information
the enzyme expression is tissue-related with the highest expression in hemocytes and widely distributed
brenda
additional information
the PtSPH1 transcript is mainly expressed in stomach, no expression in heart, hepatopancreas and muscle; the PtSP mRNA is mainly distributed in hemocytes, gill and eyestalk, very low expression in hepatopancreas and stomach, no expression in muscle
brenda
additional information
the PtSPH1 transcript is mainly expressed in stomach, no expression in heart, hepatopancreas and muscle; the PtSP mRNA is mainly distributed in hemocytes, gill and eyestalk, very low expression in hepatopancreas and stomach, no expression in muscle
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
P00771
Leptuca pugilator;
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
23000
-
x * 23000, SDS-PAGE
23500
calculated from sequence
24100
-
x * 24100, SDS-PAGE
27000
Novoden modestrus
-
gel filtration
30000
-
x * 30000, SDS-PAGE, protease A
24000
-
amino acid sequence
24000
-
x * 24000, SDS-PAGE, protease C
25000
-
sedimentation-equilibrium centrifugation
25000
-
gel filtration, ultracentrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 23000, SDS-PAGE
?
-
x * 24000, SDS-PAGE, protease C; x * 30000, SDS-PAGE, protease A
monomer
-
1 * 23000-26000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
monomer
Novoden modestrus
-
1 * 27000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
lipoprotein
the enzyme contains an N-myristoylation site
phosphoprotein
the enzyme contains potential phosphorylation sites, e.g. a casein kinase II phosphorylation site and a kinase C phosphorylation site
additional information
-
the enzme contains a putative ATP/GTP-binding site motif A, i.e. the P-loop, amino acid residues 17-24
additional information
the enzme contains a putative ATP/GTP-binding site motif A, i.e. the P-loop, amino acid residues 17-24
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.5
-
irreversible loss of activity below
36548
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
room temperature, over one month
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
mixture of collagenolytic proteases
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, real-time quantitative PCR expression analysis
gene SP, DNA and amino acid sequence determination and analysis, genomic organization, sequence comparison and phylogenetic analysis, quantitative real-time PCR expression analysis; gene SPH, DNA and amino acid sequence determination and analysis, genomic organization, sequence comparison and phylogenetic analysis, quantitative real-time PCR expression analysis
zymogen form expressed in Saccharomyces cerevisiae
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
the enzyme expression, encoded by a immune-related gene, is highly responsive to Vibrio anguillarum challenge in hemocytes/the hepatopancreas, and shows a different response to the intruding pathogens, overview
the enzyme variant PtSP shows slight increase during the first 48 h compared to control groups except 8 h point after Micrococcus luteus challenge; the expression level of enzyme variant PtSPH1 is challenged by Gram-negative bacteria Vibrio alginolyticus, Gram-positive bacteria Micrococcus luteus and fungi Pichia pastoris during the first 48 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COG2_CARMA
17
1817
Swiss-Prot
COG2_CHIOP
20
2150
Swiss-Prot
COG3_CHIOP
20
2116
Swiss-Prot
COGA_PARCM
20
2116
Swiss-Prot
COGB_PARCM
20
2150
Swiss-Prot
COGC_PARCM
20
2129
Swiss-Prot
COGS_LEPPG
226
23511
Swiss-Prot
COG1_CHIOP
20
2204
Swiss-Prot
COG1_PARCM
20
2088
Swiss-Prot
B7QAJ8_IXOSC
191
20894
TrEMBL
E9GLZ6_DAPPU
302
31592
TrEMBL
E9GLZ3_DAPPU
302
31366
TrEMBL
E9GLY9_DAPPU
304
32875
TrEMBL
E9GM00_DAPPU
309
32725
TrEMBL
Q27824_LEPPG
270
28170
TrEMBL
E9GLZ2_DAPPU
305
32589
TrEMBL
E9GLY7_DAPPU
302
32210
TrEMBL
E9GLZ1_DAPPU
302
31813
TrEMBL
E9GLZ0_DAPPU
301
32049
TrEMBL
I6LWU3_ERISI
270
28498
TrEMBL
Q8WR11_PARCM
270
28158
TrEMBL
H8Y6I6_PORTR
411
44440
TrEMBL
H8Y6I5_PORTR
286
30828
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Welgus, H.G.; Grant, G.A.
Degradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator
Biochemistry
22
2228-2233
1983
Leptuca pugilator
brenda
Grant, G.A.; Sacchettiui, J.C.; Welgus, H.G.
A collagenolytic serine protease with trypsin-like specificity from the fiddler crab Uca pugilator
Biochemistry
22
354-358
1983
Leptuca pugilator
brenda
Welgus, H.G.; Grant, G.A.; Jeffrey, J.J.; Eisen, A.Z.
Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates
Biochemistry
21
5183-5189
1982
Leptuca pugilator
brenda
Grant, G.A.; Eisen, A.Z.; Bradshaw, R.A.
Collagenolytic protease from fiddler crab (Uca pugilator)
Methods Enzymol.
80
722-734
1981
Leptuca pugilator
-
brenda
Grant, G.A.; Eisen, A.Z.
Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates
Biochemistry
19
6089-6095
1980
Leptuca pugilator
brenda
Grant, G.A.; Henderson, K.O.; Eisen, A.Z.; Bradshaw, R.A.
Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator
Biochemistry
19
4653-4659
1980
Leptuca pugilator
brenda
Eisen, A.Z.; Henderson, K.O.; Jeffrey, J.J.; Bradshaw, R.A.
A collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. Purification and properties
Biochemistry
12
1814-1822
1973
Leptuca pugilator
brenda
Eisen, A.Z.; Jeffrey, J.J.
An extractable collagenase from crustacean hepatopancreas
Biochim. Biophys. Acta
191
517-526
1969
Leptuca pugilator
brenda
Kristjansson, M.M.; Gudmundsdottir, S.; Fox, J.W.; Bjarnason, J.B.
Characterization of a collagenolytic serine proteinase from the Atlantic cod (Gadus morhua)
Comp. Biochem. Physiol. B
110
707-717
1995
Gadus morhua
brenda
Roy, P.; Colas, B.; Durand, P.
Purification, kinetical and molecular characterizations of a serine collagenolytic protease from greenshore crag (Carcinus maenas) digestive gland
Comp. Biochem. Physiol. B
115
87-95
1996
Carcinus maenas
brenda
Sellos, D.; van Wormhoudt, A.
Polymorphism and evolution of collagenolytic serine protease genes in crustaceans
Biochim. Biophys. Acta
1432
419-424
1999
Litopenaeus vannamei
brenda
Tsu, C.A.; Perona, J.J.; Schellenberger, V.; Turck, C.W.; Craik, C.S.
The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites
J. Biol. Chem.
269
19565-19572
1994
Leptuca pugilator
brenda
Tsu, C.A.; Craik, C.S.
Substrate recognition by recombinant serine collagenase 1 from Uca pugilator
J. Biol. Chem.
271
11563-11570
1996
Leptuca pugilator
brenda
Klimova, O.A.; Borukhov, S.I.; Solovyeva, N.I.; Balevskaya, T.O.; Strongin, A.Y.
The isolation and properties of collagenolytic proteases from crab hepatopancreas
Biochem. Biophys. Res. Commun.
166
1411-1420
1990
Paralithodes camtschaticus
brenda
Sakharov, I.Y.; Litvin, F.E
Artyukov, A.A.: Purification and characterization of two serine collagenolytic proteases from crab Paralithodes camtschatica
Comp. Biochem. Physiol. B
108
561-568
1994
Paralithodes camtschaticus
brenda
Lu, P.J.; Liu, H.C.; Tsai, I.H.
The midgut trypsins of shrimp (Penaeus monodon)
Biol. Chem.
371
851-859
1990
Penaeus monodon
brenda
Kim, S.K.; Park, P.J.; Kim, J.B.; Shahidi, F.
Purification and characterization of a collagenolytic protease from the filefish, Novoden modestrus
J. Biochem. Mol. Biol.
35
165-171
2002
Novoden modestrus
brenda
Rudenskaya, G.N.; Kislitsin, Y.A.; Rebrikov, D.V.
Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes
BMC Struct. Biol.
4
2-2
2004
Paralithodes camtschaticus, Paralithodes camtschaticus (Q8WR11)
brenda
Perera, E.; Pons, T.; Hernandez, D.; Moyano, F.J.; Martinez-Rodriguez, G.; Mancera, J.M.
New members of the brachyurins family in lobster include a trypsin-like enzyme with amino acid substitutions in the substrate-binding pocket
FEBS J.
277
3489-3501
2010
Panulirus argus
brenda
Li, Q.; Cui, Z.; Liu, Y.; Wang, S.; Song, C.
Identification and characterization of two novel types of non-clip domain serine proteases (PtSP and PtSPH1) from cDNA haemocytes library of swimming crab Portunus trituberculatus
Fish Shellfish Immunol.
32
683-692
2012
Portunus trituberculatus (H8Y6I5), Portunus trituberculatus (H8Y6I6), Portunus trituberculatus
brenda
Yang, Q.Z.; Yang, Z.J.; Zhang, Y.; Li, X.L.; Zhang, W.
Molecular characteristic and expression analysis of collagenolytic serine protease from the Chinese mitten crab Eriocheir sinensis with defense response to Vibrio anguillarum challenge
Genet. Mol. Res.
13
3885-3894
2014
Eriocheir sinensis, Eriocheir sinensis (I6LWU3)
brenda
html completed