Information on EC 3.4.21.4 - trypsin and Organism(s) Homo sapiens

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Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.4.21.4
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RECOMMENDED NAME
GeneOntology No.
trypsin
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nocardicin A biosynthesis
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CAS REGISTRY NUMBER
COMMENTARY hide
9002-07-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and regulates its activity, near-irreversible binding, modeling, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-4-guanidinobenzoate + H2O
4-methylumbelliferol + 4-guanidinobenzoate
show the reaction diagram
-
-
-
-
?
alpha-casein + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-DL-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-DL-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
beta-lactoglobulin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
enhanced green fluorescent protein-T1 + H2O
?
show the reaction diagram
-
enhanced green fluorescent protein-T1 is specifically cleaved into two major fragments by trypsin at the grafted cleavage site, approximately 20 and 8 kDa
-
-
?
enhanced green fluorescent protein-T1nb + H2O
?
show the reaction diagram
-
-
-
-
?
enhanced green fluorescent protein-T2 + H2O
?
show the reaction diagram
-
enhanced green fluorescent protein-T2 is specifically cleaved into two major fragments by trypsin at the grafted cleavage site, approximately 18 and 10 kDa
-
-
?
epithelial sodium channel + H2O
?
show the reaction diagram
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epithelial sodium channel cleavage and activation by isoform trypsin IV but not by trypsin I requires a critical cleavage site, i.e. Lys189 in the extracellular domain of the gamma-subunit
-
?
GDDSTPSILPAPRGYPGQV + H2O
GDDSTPSILPAPR + GYPGQV
show the reaction diagram
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-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Glu-Gly-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Gly-Pro-Arg-p-nitroanilide + H2O
Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
high pathogenic hemagglutinin + H2O
?
show the reaction diagram
-
-
-
-
?
human cartilage collagen type II + H2O
?
show the reaction diagram
inter-alpha-trypsin inhibitor heavy chain H4 + H2O
?
show the reaction diagram
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inter-alpha-trypsin inhibitor heavy chain H4 is also a marker of acute ischemic stroke
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?
L-Phe-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Pro-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
low pathogenic hemagglutinin + H2O
?
show the reaction diagram
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-
-
-
?
N-(p-tosyl)-Gly-Pro-Arg 4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-GTNRSSKGRSLIGKVDGTSHVTGKGVT-amide + H2O
SLIGKVDGTSHVTGKGVT-amide + N-acetyl-GTNRSSKGR
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-DL-arginine 4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine methyl ester + H2O
N-benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine + methanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine-4-nitroanilide + H2O
N-benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-carbobenzyloxy-Gly-Pro-Arg-p-nitroanilide + H2O
N-carbobenzyloxy-Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
NATLDPRSFLLRNPNDKYE + H2O
NATLDPR + SFLLRNPNDKYE
show the reaction diagram
-
-
-
-
?
pro-human defensin-5 + H2O
human defensin-5 + pro-human defensin-5 propeptide
show the reaction diagram
-
pro-human defensin-5 in the intestinal lumen is processed by trypsin in a complex in which chymotrypsinogen is also cleaved for activation
-
-
?
proteinase-activated receptor 1 + H2O
?
show the reaction diagram
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-
-
-
?
proteinase-activated receptor PAR-1 + H2O
activated proteinase-activated receptor PAR-1
show the reaction diagram
-
no activation by mesotrypsin in epithelial cells, but mesotrypsin activates PAR-1 in astrocytoma cells. Half-maximal response for both cationic and anionic trypsin at about 10-20 nM
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?
proteinase-activated receptor PAR-2 + H2O
activated proteinase-activated receptor PAR-2
show the reaction diagram
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no activation by mesotrypsin in epithelial cells. Half-maximal response for both cationic and anionic trypsin at about 5 nM
-
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?
proteinase-activated receptor PAR-3 + H2O
activated proteinase-activated receptor PAR-3
show the reaction diagram
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no activation by mesotrypsin in epithelial cells. Half-maximal response for both cationic and anionic trypsin at about 10-20 nM
-
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?
S-2222 + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
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?
tosyl-GPK-p-nitroanilide + H2O
tosyl-GPK + p-nitroaniline
show the reaction diagram
-
-
-
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?
tosyl-GPR-p-nitroanilide + H2O
tosyl-GPR + p-nitroaniline
show the reaction diagram
-
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-
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?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
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?
Z-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
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?
Z-Gly-Pro-Arg-p-nitroanilide + H2O
Z-Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
additional information
?
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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
enhanced green fluorescent protein-T1 + H2O
?
show the reaction diagram
-
enhanced green fluorescent protein-T1 is specifically cleaved into two major fragments by trypsin at the grafted cleavage site, approximately 20 and 8 kDa
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?
enhanced green fluorescent protein-T2 + H2O
?
show the reaction diagram
-
enhanced green fluorescent protein-T2 is specifically cleaved into two major fragments by trypsin at the grafted cleavage site, approximately 18 and 10 kDa
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
human cartilage collagen type II + H2O
?
show the reaction diagram
-
use of enzyme and its regulators as markers of prognosis and disease activity in rheumatoid arthritis
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha1-antitrypsin
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alpha1-antitrypsin Pittsburgh
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effective inhibitor, variant of alpha1-antitrypsin containing an Arg residue in place of the P1 Met358 in the reactive-site peptide bond
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Aprotinin
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very efficient inhibition of trypsin-1 and trypsin-2, but not of trypsin-4
Bauhinia variegata var. variegata trypsin inhibitor
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i.e. BvvTI, a Kunitz-type inhibitor from seeds of the Camel’s foot tree, Bauhinia variegata var. variegata. The inhibitor is also capable of significant inhibition of the proliferation of nasopharyngeal cancer CNE-1 cells in a selective way and of inhibiting anti-HIV-1 reverse transcriptase activity, overview
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clispin
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a Clitocybe nebularis trypsin inhibitor variant, recombinantly expressed in Escherichia coli, highly specific towards trypsin, fast-acting, and tight-binding. Molecular cloning of the gene and cDNA encoding cnispin, overview
Clitocybe nebularis trypsin inhibitor
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CnSPI, several inhibitor variants, separation by trypsin affinity chromatography. Possible regulatory role for CnSPIs in the endogenous proteolytic system of Clitocybe nebularis. Isolation from frozen fruiting bodies or basidiocarps
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LEKTI
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the LEKI gene encodes a 15-domain serine proteinase inhibitor, disulfide bonds are important for LEKTI function, noncompetitive mechanism, expression and purification of human LEKTI gene in Sf9
leupeptin
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nexin-1
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nexin-1 inhibits isozymes trypsin-1 ad trypsin-2, nexin-1 inhibits trypsin-4 and forms stable complexes only with this trypsin isoenzyme
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Pefabloc SC
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completely inhibits isoenzymes trypsin-1, trypsin-2, and trypsin-4
Soybean trypsin inhibitor
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-
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SVIGCWTKSIPPRPCFVK-amide
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HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTKSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the wild-type K (Lys8) residue in the presumed P1 position and is a potent, competitive, and reversible inhibitor of trypsin
SVIGCWTRSIPPRPCFVK-amide
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HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTRSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the mutant R (Arg8) residue in the presumed P1 position and is a competitive, and reversible inhibitor of trypsin with reduced potency compared to the wild type peptide SVIGCWTKSIPPRPCFVK-amide
tumor-associated trypsin inhibitor
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urinary trypsin inhibitor
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also known as ulinastatin
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
caerulein
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trypsinogen activation to trypsin occurs with 10 nM caerulein, trypsinogen is activated to reach a trypsin level of 6 nM following 10 nM caerulein induction for 1 h
enterokinase
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trypsinogens (0.0002 mM) are incubated at room temperature with 6-200 ng enterokinase in 0.1 M Tris (pH 8), containing 5 mM CaCl2 and 0.01% bovine serum albumin for 10-60 min
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additional information
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tryptase expression in human skin is significantly increased at 24 and 48 h postirradiation with ultraviolet, infrared, and heat treatment
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07744
benzoyl-DL-Arg-7-amido-4-methylcoumarin
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in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
3
benzoyl-DL-Arg-p-nitroanilide
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
0.00399
enhanced green fluorescent protein-T1
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
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0.00421
enhanced green fluorescent protein-T1nb
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in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
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0.485
Glu-Gly-Arg-4-nitroanilide
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pH 7.4, 25°C
0.0135 - 0.0274
N-carbobenzyloxy-Gly-Pro-Arg-p-nitroanilide
0.00927
tert-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
0.0141 - 0.346
Z-Gly-Pro-Arg-p-nitroanilide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
benzoyl-DL-Arg-7-amido-4-methylcoumarin
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in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
1.33
benzoyl-DL-Arg-p-nitroanilide
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
0.26
enhanced green fluorescent protein-T1
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
-
0.85
enhanced green fluorescent protein-T1nb
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
-
23.5 - 70.5
N-benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine-4-nitroanilide
-
110 - 162
N-carbobenzyloxy-Gly-Pro-Arg-p-nitroanilide
1.41
tert-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
3.86 - 88.2
Z-Gly-Pro-Arg-p-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000031
clispin
-
pH 8.0, 37°C
0.000849
LEKTI
-
pH 7.4, 25°C
0.000031
leupeptin
-
in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C
0.0000188
SVIGCWTKSIPPRPCFVK-amide
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in 10 mM phosphate buffer, pH 7.4, containing 2.7 mM KCl and 137 mM NaCl, at 37°C
0.0000542
SVIGCWTRSIPPRPCFVK-amide
-
in 10 mM phosphate buffer, pH 7.4, containing 2.7 mM KCl and 137 mM NaCl, at 37°C
additional information
additional information
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pseudo-first-order inhibition kinetics for trypsin, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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protease activity assay at
7.6
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assay at
7.8
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esterase activity assay at
8
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assay at
8.2
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assay at
8.8
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autodigestion assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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enhanced green fluorescent protein-T1 can be cleaved by trypsin under buffer conditions from pH 5 to pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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isoform trypsin IV is expressed in human renal epithelial cells and can increase epithelial sodium channel-mediated sodium transport in cultured human airway epithelial cells
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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peripheral blood
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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of rheumatoid arthritis synovial membrane
Manually annotated by BRENDA team
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fibroblast-like synovial lining of rheumatoid arthritis synovial membrane
Manually annotated by BRENDA team
additional information
-
trypsinogen is expressed in various other healthy and malignant tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
trypsin is produced as a proenzyme, trypsinogen, mainly by the pancreas, and it is activated in the gastrointestinal tract by enterokinase
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and protects it against autodigestion. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. The peptide-trypsin complex is dissociated in presence of high concentration of substrates
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enzyme immobilization in the layer structure of polyelectrolyte microcapsules leads to activity reduction of up to 90%
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA Sepharose column chromatography and Resource S column chromatography
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Q Sepharose Fast Flow column chromatography and Phenyl Sepharose Fast Flow column chromatography
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SP-Sepharose column chromatography
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trypsin 1
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21(DE3)pLysS
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inactive trypsinogen-4 is expressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R193F
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the mutation does not affect the activation energy of the reaction, but significantly alters the preexponential term of the Arrhenius equation
R193G/G142A
-
reduced activity
R193G/G184A
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reduced activity
R193G/G19A
-
reduced activity, completely resistant to chymotryptic degradation
R193Y
-
the mutation does not affect the activation energy of the reaction, but significantly alters the preexponential term of the Arrhenius equation
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
denatured trypsinogen is rapidly diluted with re-folding buffer (0.7 M guanidine-HCl, 0.1 M Tris-HCl, pH 8.0, containing 10 mM benzamidine, 2 mM L-cysteine, and 1 mM L-cystine)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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use of enzyme and its regulators as markers of prognosis and disease activity in rheumatoid arthritis