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Information on EC 3.4.21.7 - plasmin and Organism(s) Bos taurus

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.7 plasmin
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Bos taurus
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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Preferential cleavage: Lys-/- > Arg-/-; higher selectivity than trypsin. Converts fibrin into soluble products
Synonyms
plasminogen, plasmin, fibrinolysin, actase, thrombolysin, fibrinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
actase
-
-
-
-
fibrinase
fibrinolysin
plasminogen
-
-
serum tryptase
-
-
-
-
thrombolysin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-90-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-lactalbumin + H2O
?
show the reaction diagram
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
alphaS-casein + H2O
?
show the reaction diagram
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
alphas1-casein + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
beta-lactoglobulin + H2O
?
show the reaction diagram
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
Boc-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-valyl-L-leucyl-L-lysine-4-nitroanilide + H2O
D-valyl-L-leucyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
epithelial sodium channel gamma subunit + H2O
?
show the reaction diagram
-
plasmin activates epithelial sodium channels in association with inducing cleavage of the gamma subunit at gammaLys194, a site distal to the furin site. A gammaK194A mutant epithelial sodium channel subunit prevents both plasmin-dependent activation of epithelial sodium channel and plasmin-dependent production of a unique 70-kDa carboxyl-terminal gamma subunit cleavage fragment
-
-
?
kappa-casein + H2O
?
show the reaction diagram
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
lactoferrin + H2O
?
show the reaction diagram
-
hydrolysis is highly dependent on photooxidation state of substrate
-
-
?
Lys-Thr-Phe-Lys-Gly-Gly-Gly-Gly-Gly-Gly-Cys + H2O
Lys-Thr-Phe-Lys + Gly-Gly-Gly-Gly-Gly-Gly-Cys
show the reaction diagram
-
-
-
-
?
N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-L-alanyl-L-phenylalanyl-L-lysyl-7-amido-4-methylcoumarin + H2O
N-succinyl-L-alanyl-L-phenylalanyl-L-lysine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
?
epithelial sodium channel gamma subunit + H2O
?
show the reaction diagram
-
plasmin activates epithelial sodium channels in association with inducing cleavage of the gamma subunit at gammaLys194, a site distal to the furin site. A gammaK194A mutant epithelial sodium channel subunit prevents both plasmin-dependent activation of epithelial sodium channel and plasmin-dependent production of a unique 70-kDa carboxyl-terminal gamma subunit cleavage fragment
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-lactalbumin
-
shows a strong correlation with plasmin activity and may have inhibitory activity against plasmin
-
beta-Lactoglobulin
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native and denatured beta-lactoglobulin inhibits activity with D-Val-L-Leu-L-Lys-p-nitroanilide and casein
-
Blood serum
-
bovine or ovine blood serum do not affect hydrolysis of caseins in milk by plasmin. Equine and particularly porcine serum strongly inhibit casein hydrolysis. Heated serum (70°C for 5 min) from any of the species does not influence plasmin-induced hydrolysis of caseins. Bovine or ovine serum (2%) have no effect on plasmin activity when assayed on N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk. 2.0% porcine serum reduces plasmin activity on this peptide by ca. 40%
-
Protein C inhibitor
-
from Bos taurus
-
additional information
-
thermosonication at an average power of 115 W for 3 min decreases the total plasmin activity by nearly 94% in fresh skim milk and cream
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Blood serum
-
2.0% equine serum increases plasmin activity by ca.50% when assayed with N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk
-
additional information
-
the increased activity of plasmin after diafiltration may be also due to elimination of small enzyme inhibitor proteins
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
the enzyme activity follows Michaelis-Menten kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
Protein C inhibitor
-
37°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 6.6
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135 - 140
-
the enzyme activity is reduced by less than 99% in ultra-high temperature processing (140°C, 5 s or 135 °C, 2 s). Preheating at 80-95°C for 180 to 30 s lowers the enzyme activity further
57 - 70
-
heating milk at temperatures around 57°C increases the plasmin activity in the final milk product, due to increased activation of unfolded plasminogen. Thermal inactivation of plasmin starts at 65-70°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pasteurization of whey protein-free retentate of micro- and difiltrated milk at 95°C for 15 s does not significantly affect plasmin or plasminogen-derived activities. The retentate contains increased plasmin activity, proportional to the concentration of beta-lactoglobulin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLMN_BOVIN
812
0
91216
Swiss-Prot
Secretory Pathway (Reliability: 1)
E1B726_BOVIN
812
0
91243
TrEMBL
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the light chain of 50000 Da, determined by SDS-PAGE results in two bands of 30000 Da and 26000 Da
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
activation through cleavage by urokinase-type plasminogen activator is stimulated by the bacterial protease m3/6 from Pseudomonas fluorescens
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
denaturation above 65°C, thermal stability of plasmin in milk is very much dependent upon its interaction with beta-lactoglobulin
85
-
heating the enzyme in phosphate buffer medium to 85°C for 5 min can completely inactivate the enzyme
90
-
stable for 108 min in acid whey and 0.02 min in sweet whey
95
-
pasteurization of whey protein-free retentate of micro- and difiltrated milk at 95°C for 15 s does not significantly affect plasmin or plasminogen-derived activities. The retentate contains increased plasmin activity, proportional to the concentration of beta-lactoglobulin
additional information
-
the increased activity of plasmin after heat treatment may be also due to inactivation of enzyme inhibitor proteins
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, enzyme in raw milk, 10 days, the enzyme keeps a relatively constant level of activity
-
37°C, enzyme in milk products, 16 days, enzyme activity is decreased
-
4-37°C, isolated plasmin in NaCl solution, enzyme activity is lost
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
effect of plasmin on in vitro embryo production. Plasmin added to the 18 h in vitro maturation medium increases the maturation rate of embryos without affecting fertilization or embryo development rates
food industry
nutrition
-
hydrolysis of milk proteins alphaS-casein, beta-casein, kappa-casein, alpha-lactalbumin, beta-lactoglobulin, and lactoferrin is highly dependent on photooxidation state of substrate. Changes in the formation of potential angiotensin I-converting enzyme-inhibitory peptides as well as peptides proposed to have anti-bactericidal activities are observed after oxidation of substrates before plasmin hydrolysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Benfeldt, C.; Larsen, L.B.; Rasmussen, J.T.; Andreasen, P.A.; Petersen, T.E.
Isolation and characterization of plasminogen and plasmin from bovine milk
Int. Dairy J.
5
577-592
1995
Bos taurus
Manually annotated by BRENDA team
Bastian, E.D.; Hansen, K.G.; Brown, R.J.
Inhibition of plasmin by beta-lactoglobulin using casein and a synthetic substrate
J. Dairy Sci.
76
3354-3361
1993
Bos taurus
Manually annotated by BRENDA team
Yuasa, H.; Tanaka, H.; Hayashi, T.; Wakita, T.; Nakamura, H.; Nishioka, J.; Kawarada, Y.; Suzuki, K.
Bovine protein C inhibitor has a unique reactive site and can transiently inhibit plasmin
Thromb. Haemost.
83
262-267
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Crudden, A.; Oliveira, J.C.; Kelly, A.L.
Kinetic studies of the thermal inactivation of plasmin in acid or sweet whey
Int. Dairy J.
15
1245-1253
2005
Bos taurus
Manually annotated by BRENDA team
Huppertz, T.; Uniacke, T.; Kelly, A.L.; Fox, P.F.
Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum
Int. dairy J.
16
691-696
2006
Bos taurus
Manually annotated by BRENDA team
Crudden, A.; Oliveira, J.C.; Kelly, A.L.
Kinetics of changes in plasmin activity and proteolysis on heating milk
J. Dairy Res.
72
493-504
2005
Bos taurus
Manually annotated by BRENDA team
Borda, D.; Indrawati, D.; Smout, C.; Van Loey, A.; Hendrickx, M.
High pressure thermal inactivation kinetics of a plasmin system
J. Dairy Sci.
87
2351-2358
2004
Bos taurus
Manually annotated by BRENDA team
Frohbieter, K.A.; Ismail, B.; Nielsen, S.S.; Hayes, K.D.
Effects of Pseudomonas fluorescens M3/6 bacterial protease on plasmin system and plasminogen activation
J. Dairy Sci.
88
3392-3401
2005
Bos taurus
Manually annotated by BRENDA team
Passero, C.J.; Mueller, G.M.; Rondon-Berrios, H.; Tofovic, S.P.; Hughey, R.P.; Kleyman, T.R.
Plasmin activates epithelial Na+ channels by cleaving the gamma subunit
J. Biol. Chem.
283
36586-36591
2008
Bos taurus
Manually annotated by BRENDA team
Dalsgaard, T.K.; Heegaard, C.W.; Larsen, L.B.
Plasmin digestion of photooxidized milk proteins
J. Dairy Sci.
91
2175-2183
2008
Bos taurus
Manually annotated by BRENDA team
Papanikolaou, T.; Amiridis, G.S.; Dimitriadis, I.; Vainas, E.; Rekkas, C.A.
Effect of plasmin, plasminogen activators and a plasmin inhibitor on bovine in vitro embryo production
Reprod. Fertil. Dev.
20
320-327
2008
Bos taurus
Manually annotated by BRENDA team
Aaltonen, T.; Ollikainen, P.
Effect of microfiltration of milk on plasmin activity
Int. Dairy J.
21
193-197
2011
Bos taurus
Manually annotated by BRENDA team
Stoeckel, M.; Lidolt, M.; Stressler, T.; Fischer, L.; Wenning, M.; Hinrichs, J.
Heat stability of indigenous milk plasmin and proteases from Pseudomonas A challenge in the production of ultra-high temperature milk products
Int. Dairy J.
61
250-261
2016
Bos taurus
-
Manually annotated by BRENDA team
Vijayakumar, S.; Grewell, D.; Annandarajah, C.; Benner, L.; Clark, S.
Quality characteristics and plasmin activity of thermosonicated skim milk and cream
J. Dairy Sci.
98
6678-6691
2015
Bos taurus
Manually annotated by BRENDA team
Poturnayova, A.; Karpisova, I.; Castillo, G.; Mezo, G.; Kocsis, L.; Csámpai, A.; Keresztes, Z.; Hianik, T.
Detection of plasmin based on specific peptide substrate using acoustic transducer
Sens. Actuators B Chem.
223
591-598
2016
Bos taurus
-
Manually annotated by BRENDA team