Information on EC 3.4.21.32 - brachyurin

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.4.21.32
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RECOMMENDED NAME
GeneOntology No.
brachyurin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
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endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-01-8
not distinguished from EC 3.4.21.34, EC 3.4.21.35
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
greenshore crab
-
-
Manually annotated by BRENDA team
collected from the Xinxiang aquatic product market from September to October 2012 in Xinxiang, China
UniProt
Manually annotated by BRENDA team
atlantic cod
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-
Manually annotated by BRENDA team
Novoden modestrus
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
shrimp
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-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide + H2O
?
show the reaction diagram
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-
-
-
?
N-benzoyl-L-Arg-p-nitroanilide + H2O
?
show the reaction diagram
N-benzoyl-L-Tyr ethyl ester + H2O
?
show the reaction diagram
N-benzoyl-L-Tyr-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide + H2O
?
show the reaction diagram
Nalpha-tosyl-L-Arg methyl ester + H2O
?
show the reaction diagram
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-
-
-
?
succinyl-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide + H2O
?
show the reaction diagram
additional information
?
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-
substrate succinyl-Ala-Ala-Pro-Xaa-p-nitroanilide for testing substrate specificity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
Novoden modestrus
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0.06 mM, activation to 119% of control
Ca2+
Novoden modestrus
-
0.06 mM, activation to 135% of control
Co2+
-
activates
K+
Novoden modestrus
-
0.06 mM, activation to 123% of control
Li+
Novoden modestrus
-
0.06 mM, activation to 111% of control
Mn2+
-
activates
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloro-isocoumarin
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-
alpha1 protease inhibitor
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-
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basic pancreatic trypsin inhibitor
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Cd2+
Novoden modestrus
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0.06 mM, 29% inhibition
chicken ovoinhibitor
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-
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chymostatin
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-
Cu2+
Novoden modestrus
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0.06 mM, 26% inhibition
diisopropylfluorophosphate
ecotin
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EDTA
Novoden modestrus
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0.2 mM, 46% inhibition. 0.5 mM, 95% inhibition
Elastatinal
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His
Novoden modestrus
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0.2 mM, 51% inhibition. 0.7 nmM, 93% inhibition
leupeptin
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-
Mn2+
Novoden modestrus
-
0.06 mM, 14% inhibition
Ni2+
Novoden modestrus
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0.06 mM, 30% inhibition
Phenylmethylsulfonylfluoride
Soybean trypsin inhibitor
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tosyl-L-Leu-chloromethylketone
Novoden modestrus
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0.2 mM, complete inhibition
tosyl-Lys-CH2Cl
tosyl-Phe-CH2Cl
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protease C
Turkey ovomucoid
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-
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.044
N-acetyl-L-Ala-L-Ala-L-Ala-p-nitroanilide
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-
0.1
N-benzoyl-L-Arg-p-nitroanilide
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-
1.11
N-benzoyl-L-Tyr ethyl ester
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-
0.263
N-benzoyl-L-Tyr-p-nitroanilide
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-
0.12
N-benzoyl-L-Val-Gly-L-Arg-p-nitroanilide
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-
0.233
Nalpha-tosyl-L-Arg methyl ester
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-
0.14
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide
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-
0.09
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.4
-
protease C
1330
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protease A
10550
Novoden modestrus
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
Novoden modestrus
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hydrolysis of collagen
8 - 9.5
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-
8 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 9
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-
6.5 - 8.5
Novoden modestrus
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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 hide
LITERATURE
45 - 50
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-
55
Novoden modestrus
-
hydrolysis of collagen
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
3
calculated from sequence
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
x * 23000, SDS-PAGE
23500
calculated from sequence
24100
-
x * 24100, SDS-PAGE
27000
Novoden modestrus
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gel filtration
30000
-
x * 30000, SDS-PAGE, protease A
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
irreversible loss of activity below
36548
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
unstable above
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, over one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mixture of collagenolytic proteases
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protease A and C
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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
zymogen form expressed in Saccharomyces cerevisiae
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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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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.21.32)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)