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Information on EC 3.4.21.4 - trypsin and Organism(s) Rattus norvegicus

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.4 trypsin
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This record set is specific for:
Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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preferential cleavage: Arg-/-, Lys-/-
Synonyms
trypsin, at-ii, cationic trypsinogen, beta-trypsin, trypsin-like enzyme, mesotrypsin, trypsin a, cationic trypsin, anionic trypsinogen, anionic trypsin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-trypsin
-
-
-
-
Anionic trypsinogen
-
-
-
-
beta-trypsin
-
-
-
-
Brain trypsinogen
-
-
-
-
Cationic trypsinogen
-
-
-
-
cocoonase
-
-
-
-
Mesotrypsinogen
-
-
-
-
parenzyme
-
-
-
-
parenzymol
-
-
-
-
pseudotrypsin
-
-
-
-
SET
-
-
-
-
sperm receptor hydrolase
-
-
-
-
tripcellim
-
-
-
-
tryptar
-
-
-
-
tryptase
-
-
-
-
trypure
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9002-07-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AGPYAHSS + H2O
?
show the reaction diagram
-
trypsin N143H/E151H hydrolyzes the peptide exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency
-
-
?
benzyloxycarbonyl-Arg-thiobenzyl ester + H2O
benzyloxycarbonyl-Arg + phenylmethanethiol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Lys-thiobenzyl ester + H2O
benzyloxycarbonyl-Lys + phenylmethanethiol
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
beta-casein, mutant enzymes K188E and K188Y cleave nearly 30 new peptide bonds compared to wild-type enzyme
-
-
?
D-Val-Leu-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
GPNSKGRSLIGRLDTPYGGC + H2O
GPNSKGR + SLIGRLDTPYGGC
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Pefachrome tPA + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Arg-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Trp-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Trp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Lys-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-GPK-p-nitroanilide + H2O
tosyl-GPK + p-nitroaniline
show the reaction diagram
-
-
-
-
?
tosyl-GPR-p-nitroanilide + H2O
tosyl-GPR + p-nitroaniline
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
trypsin treatment alters a number of characteristics of KATP channel pharmacology, this may be due to action at possibly more than one site but includes the functional cleavage of the sulfonylurea receptor from the KATP channel
-
-
?
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
additional information
?
-
-
trypsin treatment alters a number of characteristics of KATP channel pharmacology, this may be due to action at possibly more than one site but includes the functional cleavage of the sulfonylurea receptor from the KATP channel
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
-
trypsin N143H/E151H hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency
Zn2+
-
trypsin N143H/E151H hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,7-bis(4-amidinobenzylidene)-cycloheptan-1-one
-
-
benzamidine
-
-
Bovine pancreatic trypsin inhibitor
-
BPTI, a natural non-specific serine protease inhibitor which possesses the ability to inhibit trypsin, the inhibitory activity of recombinant BPTI against trypsin is the same as natural BPTI, the trade name is aprotinin
-
Nalpha-tosylglycyl-3-amidino-DL-phenylalanine-methyl ester
-
-
pancreatic secretory trypsin inhibitor
-
also known as serine protease inhibitor Kazal type 1
-
urinary trypsin inhibitor
-
[4-(6-chloro-naphthalene-2-sulphonyl)piperazin-1-yl]-(3,4,5,6-tetrahydro-[2H-1,4']bipyridinyl-4-yl)-methanone
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0141 - 0.0182
benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide
0.086 - 2.1
Benzyloxycarbonyl-Lys-thiobenzyl ester
0.013 - 0.0472
Pefachrome tPA
0.00167 - 0.07
succinyl-Ala-Ala-Pro-Arg-7-amido-4-methylcoumarin
0.033 - 0.099
succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
0.00217 - 0.31
succinyl-Ala-Ala-Pro-Leu-7-amido-4-methylcoumarin
0.004 - 0.1
succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin
0.101 - 0.839
succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
0.004 - 0.78
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
0.000167
succinyl-Ala-Ala-Pro-Trp-7-amido-4-methylcoumarin
-
pH 8.0, 37°C, mutant enzyme D189S/DELTA223
0.08 - 0.2
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
112
alpha-N-benzyloxycarbonyl-Lys-thiobenzyl ester
-
wild-type enzyme
44.5 - 69.3
benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide
12.3
Benzyloxycarbonyl-Lys-thiobenzyl ester
-
mutant D189H
0.00167 - 91
succinyl-Ala-Ala-Pro-Arg-7-amido-4-methylcoumarin
95 - 163
succinyl-Ala-Ala-Pro-Arg-p-nitroanilide
0.000167 - 0.00217
succinyl-Ala-Ala-Pro-Leu-7-amido-4-methylcoumarin
0.004 - 121.2
succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin
40 - 74
succinyl-Ala-Ala-Pro-Lys-p-nitroanilide
0.004 - 0.0063
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
0.000167
succinyl-Ala-Ala-Pro-Trp-7-amido-4-methylcoumarin
-
pH 8.0, 37°C, mutant enzyme D189S/DELTA223
0.00067 - 0.08
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000247 - 0.000122
2,7-bis(4-amidinobenzylidene)-cycloheptan-1-one
0.00651 - 0.143
benzamidine
0.0000029
Bovine pancreatic trypsin inhibitor
-
recombinant inhibitor from Pichia pastoris, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, pH 7.5 containing 0.1% (w/v) bovine serum albumin, at 25°C
-
0.00000805 - 0.00871
Nalpha-tosylglycyl-3-amidino-DL-phenylalanine-methyl ester
0.00605 - 0.0445
[4-(6-chloro-naphthalene-2-sulphonyl)piperazin-1-yl]-(3,4,5,6-tetrahydro-[2H-1,4']bipyridinyl-4-yl)-methanone
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRYA_RAT
246
0
26901
Swiss-Prot
Secretory Pathway (Reliability: 3)
TRYB_RAT
246
0
26820
Swiss-Prot
Secretory Pathway (Reliability: 3)
TRY3_RAT
247
0
26269
Swiss-Prot
Secretory Pathway (Reliability: 2)
TRY4_RAT
247
0
26573
Swiss-Prot
Secretory Pathway (Reliability: 2)
PRS58_RAT
240
0
26812
Swiss-Prot
Secretory Pathway (Reliability: 2)
TRY1_RAT
246
0
25959
Swiss-Prot
Secretory Pathway (Reliability: 1)
TRY2_RAT
246
0
26228
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of variant X99rT containing the 99-loop (Glu97, Tyr99) of factor Xa, and variant X(99/175/190)rT containing the 99-loop the 175-loop (Ser172, Ser173, Phe174, Ile175) and Ala190 of factor Xa obtained in presence of benzamidine
-
X-ray crystal structure of trypsin R96H at pH 8.0 in the presence of CuCl2
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C191A
-
mutation decreases the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold
C191A/C220A
-
the mutant enzyme binds bovine pancreatic trypsin inhibitor with the same affinity as trypsin, the affinity of benzamidine is decresed 10fold and the affinity of leupeptin is decreased 100fold
C220A
-
mutation decreases the activity of trypsin by 20-200fold as measured by the ratio of turnover number to Km-value for the hydrolysis of amide substrates, ester hydrolysis is decreased by less than 10fold
D189S/DELTA223
-
double mutant trypsinogen, the recombinant proteinase lacks trypsin-like activity but aquires a rather unique selectivity, it preferentially hydrolyses peptide bonds C-terminal to tyrosyl residues. This narrow specificity should be useful in peptide-analytical applications such as sequence-specific fragmentation of large proteins prior to sequencing
K188F
-
increase of Km for Arg and Lys containing substrates, cleavage of nearly 30 new peptide bonds in beta-casein compared to the wild-type enzyme
K188W
-
increase of Km for Arg and Lys containing substrates, 3-4fold decrease in turnover number
K188Y
-
increase of Km for Arg and Lys containing substrates, cleavage of nearly 30 new peptide bonds in beta-casein compared to the wild-type enzyme
N143H/E151H
-
the mutant enzyme with the engineered metal binding site hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency
additional information
-
loss of the Cys191-Cys220 disulfide has no effect on the stability of trypsin as measured by urea denaturation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
double-mutant trypsinogen D189S/DELTA223
-
SP-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant rat trypsinogen II is produced as an alpha-factor fusion protein in a Saccharomyces cerevisiae expression system from the pYT plasmid
-
wild-type enzyme,variant X99rT containing the 99-loop (Glu97,Tyr99) of factor Xa, and variant X(99/175/190)rT containing the 99-loop the 175-loop (Ser172,Ser173, Phe174, Ile175) and Ala190 of factor Xa, expression in yeast
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the double mutant trypsinogen D189S/DELTA223 lacks trypsin-like activity but aquires a rather unique selectivity, it preferentially hydrolyses peptide bonds C-terminal to tyrosyl residues. This narrow specificity should be useful in peptide-analytical applications such as sequence-specific fragmentation of large proteins prior to sequencing
medicine
-
trypsin is the chief culprit of severe acute pancreatitis-associated multiple organ dysfunction syndromes, the pancreatic tissue bleeding and necrosis is special pathological change in pancreas autodigestive effect from digestive enzymes such as trypsin in severe acute pancreatitis, the activated trypsin destroys the pancreas itself causing pancreatic tissue bleeding and necrosis, trypsin also destroys the vascular endothelial barrier leading to highly increased vascular permeability
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, E.C.W.; Hung, S.H.; Cahoon, M.; Hedstrom, L.
The role of the Cys191-Cys220 disulfide bond in trypsin: new targets for engineering substrate specificity
Protein Eng.
10
405-411
1997
Rattus norvegicus
Manually annotated by BRENDA team
McGrath, M.E.; Haymore, B.L.; Summers, N.L.; Craik, C.S.; Fletterick, R.J.
Structure of an engineered, metal-actuated switch in trypsin
Biochemistry
32
1914-1919
1993
Rattus norvegicus
Manually annotated by BRENDA team
Willett, W.S.; Gillmor, S.A.; Perona, J.J.; Flettrick, R.J.; Craik, C.S.
Engineered metal regulation of trypsin specificity
Biochemistry
34
2172-2180
1995
Rattus norvegicus
Manually annotated by BRENDA team
Chobert, J.M.; Briant, L.; Leonil, J.; Molle, D.; Haertle, T.
Engineering of trypsin and its impact on beta-casein processing
Nahrung
42
135-138
1998
Rattus norvegicus
Manually annotated by BRENDA team
Lee, K.; Ozanne, S.E.; Rowe, I.C.M.; Hales, C.N.; Ashford, M.L.J.
The effects of trypsin on ATP-sensitive potassium channel properties and sulfonylurea receptors in the CRI-G1 insulin-secreting cell line
Mol. Pharmacol.
46
176-185
1994
Rattus norvegicus
Manually annotated by BRENDA team
Pal, G.; Patthy, A.; Antal, J.; Graf, L.
Mutant rat trypsin selectively cleaves tyrosyl peptide bonds
Anal. Biochem.
326
190-199
2004
Rattus norvegicus
Manually annotated by BRENDA team
Reyda, S.; Sohn, C.; Klebe, G.; Rall, K.; Ullmann, D.; Jakubke, H.D.; Stubbs, M.T.
Reconstructing the binding site of factor Xa in trypsin reveals ligand-induced structural plasticity
J. Mol. Biol.
325
963-977
2003
Rattus norvegicus
Manually annotated by BRENDA team
Knecht, W.; Cottrell, G.S.; Amadesi, S.; Mohlin, J.; Skaregaerde, A.; Gedda, K.; Peterson, A.; Chapman, K.; Hollenberg, M.D.; Vergnolle, N.; Bunnett, N.W.
Trypsin IV or mesotrypsin and p23 cleave protease-activated receptors 1 and 2 to induce inflammation and hyperalgesia
J. Biol. Chem.
282
26089-26100
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Marchbank, T.; Weaver, G.; Nilsen-Hamilton, M.; Playford, R.J.
Pancreatic secretory trypsin inhibitor is a major motogenic and protective factor in human breast milk
Am. J. Physiol. Gastrointest. Liver Physiol.
296
G697-G703
2009
Rattus norvegicus
Manually annotated by BRENDA team
Yang, L.; Dong, W.; He, J.; Ren, X.; Yan, W.
Expression and purification of natural N-terminal recombinant bovine pancreatic trypsin inhibitor from Pichia pastoris
Biol. Pharm. Bull.
31
1680-1685
2008
Rattus norvegicus
Manually annotated by BRENDA team
Itabashi, K.; Furuta, K.; Takahashi, T.; Ito, Y.; Katagiri, H.; Sato, K.; Kakita, A.; Watanabe, M.
Urinary trypsin inhibitor improves viability of the liver in brain-dead rats
Hepatogastroenterology
55
568-573
2008
Rattus norvegicus
Manually annotated by BRENDA team
Taie, S.; Ueki, M.; Chujo, K.; Asaga, T.; Iwanaga, Y.; Ono, J.; Maekawa, N.
Urinary trypsin inhibitor ameliorates renal tissue oxygenation after ischemic reperfusion in rats
J. Anesth.
22
149-154
2008
Rattus norvegicus
Manually annotated by BRENDA team
Sha, H.; Ma, Q.; Jha, R.K.
Trypsin is the culprit of multiple organ injury with severe acute pancreatitis
Med. Hypotheses
72
180-182
2009
Rattus norvegicus
Manually annotated by BRENDA team