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Information on EC 3.4.21.32 - brachyurin
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3.4.21.32 brachyurinSpecify your search results
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- 3.4.21.32
-
metalloproteinases
-
timp-1
- cartilage
- synovial
- fibrosis
- joint
- chondrocytes
- dermal
-
gelatinase
- arthritis
- islet
-
zymography
-
articular
- metastasis
- osteoarthritis
-
rheumatoid
- prostaglandin
- fibronectin
-
gelatin
-
elastase
-
proteoglycans
-
basement
- hyaluronidase
- plasminogen
-
interleukin-1
-
procollagen
- periodontal
- fibril
- stromelysin
- osteoblast
- tendon
-
intracerebral
- knee
- resorption
- hydroxyproline
- gingival
-
proteinases
- ligament
-
dish
- glycosaminoglycans
-
tensile
-
gelatinolytic
- calvaria
-
aggrecan
- contracture
-
fibroblast-like
- synoviocytes
- mt1-mmp
-
crevicular
-
cruciate
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
Synonyms
collagenase, mmp-1, metalloproteinase-1, matrix metalloproteinase-1, collagenase a, collagenolytic protease, collagen peptidase, collagenase mmp-1, azocollase, collagenolytic serine protease, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspergillopeptidase C
-
-
-
-
azocollase
-
-
-
-
clostridiopeptidase A
-
-
-
-
clostridiopeptidase I
-
-
-
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clostridiopeptidase II
-
-
-
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collagen peptidase
-
-
-
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collagenase
-
-
-
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collagenase A
-
-
-
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collagenase MMP-1
-
-
-
-
collagenolytic protease
-
-
-
-
collagenolytic serine protease
kollaza
-
-
-
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matrix metalloproteinase-1
-
-
-
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matrix metalloproteinase-18
-
-
-
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Matrix metalloproteinase-8
-
-
-
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metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
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MMP-1
-
-
-
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MMP-8
-
-
-
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nucleolysin
-
-
-
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peptidase, clostridio-, A
-
-
-
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proteinase, Clostridium histolyticum, A
-
-
-
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soycollagestin
-
-
-
-
uca pugilator collagenolytic proteinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-01-8
not distinguished from EC 3.4.21.34, EC 3.4.21.35
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
substrate succinyl-Ala-Ala-Pro-Xaa-p-nitroanilide for testing substrate specificity
-
-
-
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
-
calf skin collagen type III and bovine lens capsule collagen type IV
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
Novoden modestrus
-
45°C: about 40% of maximal activity, 60°C: about 45% of maximal activity, hydrolysis of collagen
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from the Xinxiang aquatic product market from September to October 2012 in Xinxiang, China
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
25000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 24000, SDS-PAGE, protease C; x * 30000, SDS-PAGE, protease A
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the enzyme contains potential phosphorylation sites, e.g. a casein kinase II phosphorylation site and a kinase C phosphorylation site
additional information
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
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Penaeus 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
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