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Information on EC 3.4.21.20 - cathepsin G and Organism(s) Homo sapiens and UniProt Accession P08311

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.20 cathepsin G
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P08311 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
specificity similar to chymotrypsin C
Synonyms
alpha-protease, cat G, Cat-G, Cat.G, CatG, Cath G, cathepsin G, chymotrypsin-like proteinase, More, neutral proteinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cat G
247
-
Cat-G
247
-
Cath G
247
-
cathepsin G
chymotrypsin-like proteinase
-
-
-
-
neutral proteinase
-
-
-
-
serine protease cathepsin G
247
-
Vimentin-specific protease
-
-
-
-
VSP
-
-
-
-
additional information
247
the enzyme belongs to the chymotrypsin family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
specificity similar to chymotrypsin C
show the reaction diagram
active site structure
-
CAS REGISTRY NUMBER
COMMENTARY hide
56645-49-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-GIAPFCDLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFCDLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFCMLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFCPLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFCRLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFDMLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFRMLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFSMLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIATFWMLMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIEPFSDPMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIEPKSDPMPEQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIEPKSDPMPEQ-N-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-TPFSALQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-TPKSALQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-TPWSALQ-YNO2 + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + ?
show the reaction diagram
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
show the reaction diagram
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
show the reaction diagram
-
-
-
?
cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
low-density lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
4-carboxybutyryl-Phe-2-naphthyl ester + H2O
4-carboxybutyryrl-Phe + 2-naphthol
show the reaction diagram
-
-
-
ir
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-APEEIMRRQ-EDDnp + H2O
Abz-APEEI + MRRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-EPFWEDQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-VADnVRDRQ-EDDnp + H2O
Abz-VADnVR + DRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-amino-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-amino-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-carboxy-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-carboxy-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-COOCH3-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-COOCH3-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-cyano-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-cyano-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-guanidyl-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-guanidyl-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-nitro-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-nitro-L-phenylalanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Arg-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Arg + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Lys-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Lys + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Phe-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Phe + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Tyr + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
show the reaction diagram
-
chromogenic cathepsin G substrate
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
-
-
-
?
factor IX + H2O
?
show the reaction diagram
-
-
-
-
?
factor VII + H2O
?
show the reaction diagram
-
-
-
-
?
factor VIII + H2O
factor VIIIa + peptide
show the reaction diagram
factor VIIIa + H2O
factor VIII + peptide
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
fibronectin + H2O
fragments of fibronectin
show the reaction diagram
fibronectin + H2O
peptide fragments
show the reaction diagram
glycoprotein Ibalpha subunit + H2O
?
show the reaction diagram
-
from the glycoprotein Ib-IX receptor of human platelets
-
-
?
hemagglutinin + H2O
?
show the reaction diagram
-
assay at pH 5.0, 37°C
-
-
?
high molecular mass kininogen + H2O
peptide fragments
show the reaction diagram
-
human, 120 kDa
after 1 min reaction: 110, 100, and 75 kDa fragments, after 5 min reaction: 10 to 70 kDa fragments, after 60 min: less than 20 kDa fragments
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
show the reaction diagram
intercellular adhesion molecule-1 + H2O
fragments
show the reaction diagram
Laminin + H2O
?
show the reaction diagram
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
laminin + H2O
fragments of laminin
show the reaction diagram
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
show the reaction diagram
N-acetyl-L-Phe-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-N-(5-amino-2-nitrobenzoyl)-3-pyridin-4-yl-L-alaninamide) + H2O
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-3-pyridin-4-yl-L-alanine + 5-amino-2-nitrobenzamide
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-Tyr ethyl ester + H2O
N-benzoyl-L-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
show the reaction diagram
-
-
-
-
-
N-carbobenzyloxy-L-Lys-thiobenzylester + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
assay at 37°C
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
N-succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
chromogenic substrate
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Phe-Leu-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
chromogenic substrate
-
?
protease-activated receptor-1 + H2O
?
show the reaction diagram
-
i.e. PAR1, activation of platelets by hydrolysis of the receptor protein
-
?
protease-activated receptor-4 + H2O
?
show the reaction diagram
-
i.e. PAR4, activation of platelets by hydrolysis of the receptor protein
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
show the reaction diagram
succinyl-Ala-Ala-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
ir
succinyl-Phe-Leu-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
tetanus toxin C-fragment + H2O
?
show the reaction diagram
-
assay at pH 5.0, 37°C
-
-
?
thrombospondin + H2O
peptide fragments
show the reaction diagram
von Willebrand factor + H2O
peptide fragments
show the reaction diagram
additional information
?
-
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
angiotensin I + H2O
angiotensin II + ?
show the reaction diagram
P08311
-
-
-
?
angiotensinogen + H2O
angiotensin I + ?
show the reaction diagram
P08311
-
-
-
?
angiotensinogen + H2O
angiotensin II + ?
show the reaction diagram
P08311
-
-
-
?
cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
low-density lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
factor VIII + H2O
factor VIIIa + peptide
show the reaction diagram
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, overview
-
-
?
factor VIIIa + H2O
factor VIII + peptide
show the reaction diagram
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, inactivation occurs due to decreased stability by subsequent dissociation of the A2 subunit following proteolytic cleavage by cathepsin G, overview
-
-
?
fibronectin + H2O
fragments of fibronectin
show the reaction diagram
-
degradation, involved in inflammation process
-
ir
fibronectin + H2O
peptide fragments
show the reaction diagram
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
show the reaction diagram
-
i.e. hbrm, nuclear protein in volved in regulation of chromatin conformation
-
?
intercellular adhesion molecule-1 + H2O
fragments
show the reaction diagram
-
i.e. ICAM-1, the substrate plays an important role in inflammation and immune response, e.g. to sustain neutrophil infiltration and to confer susceptibility to septic shock, all alternate substrate isoforms but the common form, in model mouse mutants, and in cystic fibrosis patients
-
?
laminin + H2O
fragments of laminin
show the reaction diagram
-
degradation, involved in inflammation process
-
ir
myelin basic protein + H2O
myelin basic protein peptide fragments
show the reaction diagram
-
the serine protease cathepsin G dominates the proteolytic processing of the multiple sclerosis-associated autoantigen myelin basic protein in lysosomes from primary B cells and dendritic cells, overview
-
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
show the reaction diagram
-
cell-associated N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
thrombospondin + H2O
peptide fragments
show the reaction diagram
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
von Willebrand factor + H2O
peptide fragments
show the reaction diagram
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
enhances the ionic interaction and binding affinity and thereby increases the inhibitory effect of glycosaminiglycans and heparin-like dextran derivatives depending on the nature of chemical groups substituted to the dextran
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha1-CT
-
-
-
cathepsin G inhibitor I
-
-
-
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-chloromethylketone
-
irreversible inhibitor
N-succinyl-L-Val-L-Pro-L-Phe-(OPh)2
-
irreversible inhibitor
11-oxo-beta-boswellic acid
-
0.01 mM, 30% cathepsin G activity compared to control
2-(N-methyl)benzylamino-3,1-benzoxazin-4-one
-
strongest inhibition
2-amino-3,1-benzoxazin-4-ones
-
non-covalent complex formation, hydrophobic and basic residues at position 2, kinetics of acylation and desacylation, binding at the enzyme's active site
3-O-acetyl-11-oxo-beta-boswellic acid
-
0.01 mM, 15% cathepsin G activity compared to control
3-O-acetyl-beta-boswellic acid
-
0.01 mM, 5% cathepsin G activity compared to control
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
-
6-((1'R)-camphanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-((1'R,2'S,5'R)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-((1'S)-camphanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-((1'S,2'R,5'S)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-(benzoyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-(N-tosyl-L-phenylalanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-(N-tosyl-L-valinyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
alpha-1 proteinase inhibitor
-
-
-
alpha-1-antichymotrypsin
-
-
-
alpha1-Aantichymotrypsin
-
alpha1-protease inhibitor
-
-
-
Alpha1-proteinase inhibitor
-
-
-
alpha2-Macroglobulin
-
-
-
aspartyl protease inhibitor pepstatin
-
-
-
benzyloxycarbonyl-Gly-Leu-Phe-chloromethyl ketone
beta-boswellic acid
-
0.01 mM, 30% cathepsin G activity compared to control
bis(4-ethylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-methoxyphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
bis(4-methylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-tert-butylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis-naphthyl beta-ketophosphoric acid
-
moderately potent, competitive, reversible, the R-isomer occupies the active site of the enzyme
bis[4-(1,1,3,3-tetramethylbutyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
3% inhibition, 115 microM
bis[4-(1-methylethyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] ([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][(O-tert-butyl-L-threonyl)amino]methyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl]([O-tert-butyl-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-threonyl]amino)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
CatG-specific inhibitor I
-
reversible inhibitor
-
cathepsin G inhibitor I
-
-
-
chelonianin
-
-
-
chymostatin
-
-
chymotrypsin inhibitor 1
-
Apis mellifera
-
chymotrypsin inhibitor 2
-
Apis mellifera
-
chymotrypsin inhibitor 3
-
Apis mellifera
-
cysteine protease inhibitor E64
-
-
dermatan sulfate
-
25 kDa, protection of laminin and fibronectin against degradation by cathepsin G
dichloroisocoumarin
-
-
diethyl 1-naphthylmethylphosphonate
-
-
diisopropylfluorophosphate
-
-
dinaphthalen-2-yl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
-
diphenyl (4-amino-1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
5% inhibition, 221 microM
diphenyl [(4-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
-
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidoylphenyl)methyl]phosphonate
-
30% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](6-carbamimidoylnaphthalen-2-yl)methyl]phosphonate
-
5% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](phenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
ecotin
-
-
-
glut-11-oxo-beta-boswellic acid
-
0.01 mM 20% cathepsin G activity compared to control
heparan sulfate
-
60 kDa, protection of laminin and fibronectin against degradation by cathepsin G
heparin
-
12 kDa, 1:1 binding stoichiometry with cathepsin G, protection of laminin and fibronectin against degradation by cathepsin G
heparin N
-
-
-
heparin S0
-
-
-
heparin S1
-
-
-
heparin S2
-
-
-
heparin S3
-
-
-
high molecular mass kininogen
-
i.e. HK, human, competitive, inhibits platelet activation by the enzyme completely by complex formation with the enzyme
-
JNJ-10311795
-
inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an opportunity in the treatment of asthma and chronic obstructive pulmonary disease
L-1-tosylamido-2-phenylethyl chloromethyl ketone
-
weak inhibition
L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
leupeptin
-
-
Lys16-aprotinin
-
-
-
monocyte neutrophil elastase inhibitor
-
-
-
mutant R346F of plasminogen activator inhibitor-1
-
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
TPCK, inhibitor of the proteolytic activity of cathepsin G, effectively eliminated cathepsin G-induced chemotaxis of monocytes
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
two times more active against cathepsin G than against trypsin
pepstatin A-penetratin
-
-
-
phenylmethylsulfonyl fluoride
-
-
plasma serine protease inhibitor ACT
-
-
-
protease inhibitor PI6
-
-
-
RG1150
-
i.e. carboxymethyl-benzylamide-dextran derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1192
-
i.e. carboxymethyl-benzylamide-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1503
-
i.e. carboxymethyl-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
secretory leukocyteprotease inhibitor
-
-
-
serpin
-
-
-
Soybean trypsin inhibitor
-
-
-
specific Cat-G inhibitor
-
1 microM, decrease of enzyme activity by 43%
-
squamous cell carcinoma antigen 2
-
-
-
thrombospondin 1
-
-
-
tosylphenylalanyl chloromethane
-
-
ursolic acid
-
0.01 mM, 80% cathepsin G activity compared to control
[2-(3-methylcarbamoyl-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
-
[2-(3-[(3-benzoylamino-propyl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
-
[2-(3-[(piperidin-4-yl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
reversible, selective, competitive inhibition
[2-(3-[methyl-(diphenyl-ethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
strong inhibition
[2-(3-[methyl-(phenethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
-
[2-(3-[methyl[1-(2-naphthoyl)piperidin-4-yl]amino]carbonyl]-2-naphthyl)-1-(1-naphthyl)-2-oxoethyl]phosphonic acid
-
0.0005 mM, 10% cathepsin G activity compared to control
[2-[3-(benzyl-methyl-carbamoyl)-naphthalen-2-yl]-1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
-
[Nphe,Npip,Nleu]SFTI-1
-
0.1 mM
-
[Phe(4-guanidine)]SFTI-1
-
0.1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-formylmethionyl-leucyl-phenylalanine
-
induces release of enzyme from neutrophils
phosphocholine
-
phospholipid vesicles containing phosphatidyl-L-serine and phosphocholine are required for enzyme-mediated thrombin production in platelet-free plasma, potentially due to protection of lipid bound enzyme from inhibition
platelet-activating factor
-
induces release of enzyme from neutrophils
additional information
-
cathepsin G activity in samples from activated lymphocytes increases slowly with age of patients, both in intra- and extracellular compartments
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0097
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0099
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0035
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0032
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0021
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
-
pH 7.5, 25°C
0.203
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
1.49
methoxysuccinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide
-
-
2.6
N-benzoyl-L-tyrosine ethyl ester
-
-
0.69 - 1.73
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.421
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2
-
pH 7.5, 25°C
0.604 - 6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
0.512
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2
-
pH 7.5, 25°C
0.524 - 6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
19
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
6
methoxysuccinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide
-
-
68.3
N-acetyl-L-phenylalanine-p-nitrophenyl ester
-
-
3
N-benzoyl-L-tyrosine ethyl ester
-
-
14 - 100
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2054
Abz-GIAPFCDLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
817
Abz-GIATFCDLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
263
Abz-GIATFCMLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
560
Abz-GIATFCPLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
68
Abz-GIATFCRLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
175
Abz-GIATFDMLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
162
Abz-GIATFRMLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
217
Abz-GIATFSMLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
69
Abz-GIATFWMLMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
1700
Abz-GIEPFSDPMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
190
Abz-GIEPKSDPMPEQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
153.8
Abz-TPFSALQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
8.1
Abz-TPKSALQ-EDDnp
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
69
Abz-TPWSALQ-YNO2
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
20 - 58
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0071
alpha-1 proteinase inhibitor
-
-
-
0.027
alpha-1-antichymotrypsin
-
-
-
0.0000008
dermatan sulfate
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.000000015
ecotin
-
-
-
0.000003
heparan sulfate
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.0000008
heparin
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.00172
heparin N
-
pH 7.4
-
0.00082
heparin S0
-
pH 7.4
-
0.00213
heparin S1
-
pH 7.4
-
0.00003
heparin S2
-
pH 7.4
-
0.00081
heparin S3
-
pH 7.4
-
0.000038
JNJ-10311795
-
-
0.27
Lys16-aprotinin
-
wild type enzyme, in 1.8 M NaCl, pH 8.0, 37°C
-
0.59
mutant R346F of plasminogen activator inhibitor-1
-
-
-
0.00000011
RG1150
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester
-
0.00000017
RG1192
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester; pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester, at physiologic ionic strength
-
0.0000012
RG1503
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, in presence of 0.1 Na+
-
0.00005 - 0.00006
[2-(3-[(piperidin-4-yl)-methyl-carbamoyl]-naphthalen-2-yl)1-naphthalen-1-yl-2-oxo-ethyl]-phosponic acid
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.02
-
healthy subjects
16.14
-
patients with ulcerative colitis and specific Cat-G inhibitor
28.34
-
patients with ulcerative colitis
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
assay at
5.5
-
assay at
7.2
-
assay at
7.5 - 8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
5.8 - 8
-
more than 50% of maximal activity at pH 5.8 and pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
40
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is expressed in intimal and medial cells, particularly abundant in atheroma plaque
Manually annotated by BRENDA team
-
myeloid dendritic cell1 and myeloid dendritic cell2
Manually annotated by BRENDA team
-
leukemic cell line
Manually annotated by BRENDA team
-
of patients with rheumatoid arthritis and osteoarthritis
Manually annotated by BRENDA team
-
rheumatoid
Manually annotated by BRENDA team
additional information
-
no activity in HeLa cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
apoptotic NB4 cells
Manually annotated by BRENDA team
-
mechanism by which the enzyme binds to activated human neutrophil plasma membranes, a functional active site is not required for binding, overview, inhibition of binding by 1. trypsin, chondroitinase ABC, and heparitinases, but not other glycanases, and by 2. purified chondroitin sulfates, heparan sulfate, and other sulfated molecules, but not by non-sulfated glycans, binding kinetics, overview
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CATG_HUMAN
255
0
28837
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
17000
-
gel filtration
26000
-
MALDI-TOF
28500
-
x * 28500
30000
-
x * 30000, SDS-PAGE
39000
-
Western blot
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
the enzyme contains one glycosylation site
side-chain modification
-
glycoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with the inhibitor JNJ-10311795, 1.85 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A226E
-
the substitution at the bottom of the cathepsin G S1 pocket allows cathepsin G to accommodate a Lys residue at P1
A226E
-
the missense mutation creates tryptic activity in human cathepsin G
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
autolysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
-20°C, lyophilized
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, elastin-Sepharose affinity chromatography, ion-exchange chromatography
-
Protein G Sepharose 4 Fast Flow
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
the gene is located at chromosome 14q11.2
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
level of cathepsin G is reduced in peripheral polymorphonuclear leukocytes of hemodialysis patients, while the mRNA enzyme level is not different
-
patients with atherosclerosis have significantly reduced plasma enzyme levels
-
both CatG activity and transcript level are elevated in peripheral blood mononuclear cells from type 1 diabetes mellitus patients. Vitamin D reduces CatG activity only in myeloid dendritic cells from healthy donors
-
higher expression of Cat-G in biopsies from patients with ulcerative colitis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a therapeutic target
medicine
-
JNJ-10311795 is an inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an exciting opportunity in the treatment of asthma and chronic obstructive pulmonary disease
pharmacology
-
structure-based drug design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tschesche, H.; Wenzel, H.R.; Engelbrecht, S.; Schnabel, E.
Cathepsin G
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
164-170
1984
Homo sapiens
-
Manually annotated by BRENDA team
Barrett, A.J.
Cathepsin G
Methods Enzymol.
80
561-565
1981
Homo sapiens
Manually annotated by BRENDA team
Heck, L.W.; Rostand, K.S.; Hunter, F.A.; Bhown, A.
Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors
Anal. Biochem.
158
217-227
1986
Homo sapiens
Manually annotated by BRENDA team
Virca, G.D.; Metz, G.; Schnebli, H.P.
Similarities between human and rat leukocyte elastase and cathepsin G
Eur. J. Biochem.
144
1-9
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Starkey, P.M.; Barrett, A.J.
Human cathepsin G
J. Biochem.
155
273-278
1976
Homo sapiens
Manually annotated by BRENDA team
Starkey, P.M.; Barret, A.J.
Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin G
Biochem. J.
155
255-263
1976
Homo sapiens
Manually annotated by BRENDA team
Braun, N.J.; Bodmer, J.L.; Virca, G.D.; Metz-Virca, G.; Maschler, R.; Bieth, J.G.; Schnebli, H.P.
Kinetic studies on the interaction of eglin c with human leukocyte elastase and cathepsin G
Biol. Chem. Hoppe-Seyler
368
299-308
1987
Homo sapiens
Manually annotated by BRENDA team
Stein, R.L.; Strimpler, A.M.
Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin
Biochemistry
26
2611-2615
1987
Homo sapiens
Manually annotated by BRENDA team
Saklatvala, J.; Barrett, A.J.
Identification of proteinases in rheumatoid synovium. Detection of leukocyte elastase cathepsin G and another serine proteinase
Biochim. Biophys. Acta
615
167-177
1980
Homo sapiens
Manually annotated by BRENDA team
Lively, M.O.; Powers, J.C.
Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides
Biochim. Biophys. Acta
525
171-179
1978
Homo sapiens
Manually annotated by BRENDA team
Powers, J.C.; Gupton, B.F.; Harley, A.D.; Nishino, N.; Whitley, R.J.
Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
Biochim. Biophys. Acta
485
156-166
1977
Homo sapiens
Manually annotated by BRENDA team
Duranton, J.; Adam, C.; Bieth, J.G.
Kinetic mechanism of the inhibition of cathepsin G by alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor
Biochemistry
37
11239-11245
1998
Homo sapiens
Manually annotated by BRENDA team
Bania, J.; Stachowiak, D.; Polanowski, A.
Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera
Eur. J. Biochem.
262
680-687
1999
Homo sapiens
Manually annotated by BRENDA team
Ermolieff, J.; Boudier, C.; Laine, A.; Meyer, B.; Bieth, J.G.
Heparin protects cathepsin G against inhibition by protein proteinase inhibitor
J. Biol. Chem.
269
29502-29508
1994
Homo sapiens
Manually annotated by BRENDA team
Pidard, D.; Renesto, P.; Berndt, M.C.; Rabhi, S.; Clemetsons, K.J.; Chignard, M.
Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit
Biochem. J.
303
489-498
1994
Homo sapiens
Manually annotated by BRENDA team
Hogg, P.J.; Owensby, D.A.; Chesterman, C.N.
Thrombospondin 1 is a tight-binding competitive inhibitor of neutrophil cathepsin G. Determination of the kinetic mechanism of inhibition and localization of cathepsin G binding to the thrombospondin 1 type 3 repeats
J. Biol. Chem.
268
21811-21818
1993
Homo sapiens
Manually annotated by BRENDA team
Groutas, W.C.; Brubaker, M.J.; Verkataraman, R.; Epp, J.B.; Stang, M.A.; McClenahan, J.J.
Inhibitors of human neutrophil cathepsin G: structural and biochemical studies
Arch. Biochem. Biophys.
294
114-146
1992
Homo sapiens
-
Manually annotated by BRENDA team
Turkington, P.T.
Cathepsin G, a regulator of human vitamin K, dependent clotting factors and inhibitors
Thromb. Res.
67
147-155
1992
Homo sapiens
Manually annotated by BRENDA team
Hof, P.; Mayr, I.; Huber, R.; Korzus, E.; Potempa, J.; Travis, J.; Powers, J.C.; Bode, W.
The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities
EMBO J.
15
5481-5491
1996
Homo sapiens
Manually annotated by BRENDA team
Maison, C.M.; Villiers, C.L.; Colomb, M.G.
Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G
J. Immunol.
147
921-926
1991
Homo sapiens
Manually annotated by BRENDA team
Gutschow, M.; Kuerschner, L.; Pietsch, M.; Ambrozak, A.; Neumann, U.; Gunther, R.; Hofmann, H.J.
Inhibition of cathepsin G by 2-amino-3,1-benzoxazin-4-ones: kinetic investigations and docking studies
Arch. Biochem. Biophys.
402
180-191
2002
Homo sapiens
Manually annotated by BRENDA team
Tani, K.; Murphy, W.J.; Chertov, O.; Oppenheim, J.J.; Wang, J.M.
The neutrophil granule protein cathepsin G activates murine T lymphocytes and upregulates antigen-specific IG production in mice
Biochem. Biophys. Res. Commun.
282
971-976
2001
Homo sapiens
Manually annotated by BRENDA team
Vagnoni, L.M.; Gronostaj, M.; Kerrigan, J.E.
6-Acylamino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-diones mechanism-based inhibitors of human leukocyte elastase and cathepsin G: effect of chirality in the 6-acylamino substituent on inhibitory potency and selectivity
Bioorg. Med. Chem.
9
637-645
2001
Homo sapiens
Manually annotated by BRENDA team
Robledo, O.; Papaioannou, A.; Ochietti, B.; Beauchemin, C.; Legault, D.; Cantin, A.; King, P.D.; Daniel, C.; Alakhov, V.Y.; Potworowski, E.F.; St-Pierre, Y.
ICAM-1 isoforms: specific activity and sensitivity to cleavage by leukocyte elastase and cathepsin G
Eur. J. Immunol.
33
1351-1360
2003
Homo sapiens
Manually annotated by BRENDA team
Ledoux, D.; Merciris, D.; Barritault, D.; Caruelle, J.P.
Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G
FEBS Lett.
537
23-29
2003
Homo sapiens
Manually annotated by BRENDA team
Selim, T.E.; Ghoneim, H.R.; Abdel Ghaffar, H.A.; Colman, R.W.; Dela Cadena, R.A.
High molecular mass kininogen inhibits cathepsin G-induced platelet activation by forming a complex with cathepsin G
Hematol. J.
2
371-377
2001
Homo sapiens
Manually annotated by BRENDA team
Greco, M.N.; Hawkins, M.J.; Powell, E.T.; Almond, H.R., Jr.; Corcoran, T.W.; de Garavilla, L.; Kauffman, J.A.; Recacha, R.; Chattopadhyay, D.; Andrade-Gordon, P.; Maryanoff, B.E.
Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design
J. Am. Chem. Soc.
124
3810-3811
2002
Homo sapiens
Manually annotated by BRENDA team
Sambrano, G.R.; Huang, W.; Faruqi, T.; Mahrus, S.; Craik, C.; Coughlin, S.R.
Cathepsin G activates protease-activated receptor-4 in human platelets
J. Biol. Chem.
275
6819-6823
2000
Homo sapiens
Manually annotated by BRENDA team
Goel, M.S.; Diamond, S.L.
Neutrophil cathepsin G promotes prothrombinase and fibrin formation under flow conditions by activating fibrinogen-adherent platelets
J. Biol. Chem.
278
9458-9463
2003
Homo sapiens
Manually annotated by BRENDA team
Moriuchi, H.; Moriuchi, M.; Fauci, A.S.
Cathepsin G, a neutrophil-derived serine protease, increases susceptibility of macrophages to acute human immunodeficiency virus type 1 infection
J. Virol.
74
6849-6855
2000
Homo sapiens
Manually annotated by BRENDA team
Biggs, J.R.; Yang, J.; Gullberg, U.; Muchardt, C.; Yaniv, M.; Kraft, A.S.
The human brm protein is cleaved during apoptosis: the role of cathepsin G
Proc. Natl. Acad. Sci. USA
98
3814-3819
2001
Homo sapiens
Manually annotated by BRENDA team
Bonnefoy, A.; Legrand, C.
Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase
Thromb. Res.
98
323-332
2000
Homo sapiens
Manually annotated by BRENDA team
Sissi, C.; Lucatello, L.; Naggi, A.; Torri, G.; Palumbo, M.
Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G
Biochem. Pharmacol.
71
287-293
2006
Homo sapiens
Manually annotated by BRENDA team
Mezyk-Kope?, R.; Bzowska, M.; Bzowska, M.; Mickowska, B.; Mak, P.; Potempa, J.; Bereta, J.
Effects of elastase and cathepsin G on the levels of membrane and soluble TNFalpha
Biol. Chem.
386
801-811
2005
Homo sapiens
Manually annotated by BRENDA team
Yui, S.; Tomita, K.; Kudo, T.; Ando, S.; Yamazaki, M.
Induction of multicellular 3-D spheroids of MCF-7 breast carcinoma cells by neutrophil-derived cathepsin G and elastase
Cancer Sci.
96
560-570
2005
Homo sapiens
Manually annotated by BRENDA team
Helske, S.; Syvaeranta, S.; Kupari, M.; Lappalainen, J.; Laine, M.; Lommi, J.; Turto, H.; Maeyraenpaeae, M.; Werkkala, K.; Kovanen, P.T.; Lindstedt, K.A.
Possible role for mast cell-derived cathepsin G in the adverse remodelling of stenotic aortic valves
Eur. Heart J.
27
1495-1504
2006
Homo sapiens
Manually annotated by BRENDA team
Tralau, T.; Meyer-Hoffert, U.; Schroeder, J.M.; Wiedow, O.
Human leukocyte elastase and cathepsin G are specific inhibitors of C5a-dependent neutrophil enzyme release and chemotaxis
Exp. Dermatol.
13
316-325
2004
Homo sapiens
Manually annotated by BRENDA team
Raptis, S.Z.; Shapiro, S.D.; Simmons, P.M.; Cheng, A.M.; Pham, C.T.
Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
Immunity
22
679-691
2005
Homo sapiens
Manually annotated by BRENDA team
Rivera-Marrero, C.A.; Stewart, J.; Shafer, W.M.; Roman, J.
The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli
Infect. Immun.
72
5712-5721
2004
Homo sapiens
Manually annotated by BRENDA team
Stefansson, S.; Yepes, M.; Gorlatova, N.; Day, D.E.; Moore, E.G.; Zabaleta, A.; McMahon, G.A.; Lawrence, D.A.
Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors
J. Biol. Chem.
279
29981-29987
2004
Homo sapiens
Manually annotated by BRENDA team
de Garavilla, L.; Greco, M.N.; Sukumar, N.; Chen, Z.W.; Pineda, A.O.; Mathews, F.S.; Di Cera, E.; Giardino, E.C.; Wells, G.I.; Haertlein, B.J.; Kauffman, J.A.; Corcoran, T.W.; Derian, C.K.; Eckardt, A.J.; Damiano, B.P.; Andrade-Gordon, P.; Maryanoff, B.E.
A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo
J. Biol. Chem.
280
18001-18007
2005
Homo sapiens, Homo sapiens (P08311)
Manually annotated by BRENDA team
Shao, B.; Belaaouaj, A.; Verlinde, C.L.; Fu, X.; Heinecke, J.W.
Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase
J. Biol. Chem.
280
29311-29321
2005
Homo sapiens
Manually annotated by BRENDA team
Legedz, L7.; Randon, J.; Sessa, C.; Baguet, J.P.; Feugier, P.; Cerutti, C.; McGregor, J.; Bricca, G.
Cathepsin G is associated with atheroma formation in human carotid artery
J. Hypertens.
22
157-166
2004
Homo sapiens
Manually annotated by BRENDA team
Burster, T.; Beck, A.; Tolosa, E.; Marin-Esteban, V.; Roetzschke, O.; Falk, K.; Lautwein, A.; Reich, M.; Brandenburg, J.; Schwarz, G.; Wiendl, H.; Melms, A.; Lehmann, R.; Stevanovic, S.; Kalbacher, H.; Driessen, C.
Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes
J. Immunol.
172
5495-5503
2004
Homo sapiens
Manually annotated by BRENDA team
Sun, R.; Iribarren, P.; Zhang, N.; Zhou, Y.; Gong, W.; Cho, E.H.; Lockett, S.; Chertov, O.; Bednar, F.; Rogers, T.J.; Oppenheim, J.J.; Wang, J.M.
Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor
J. Immunol.
173
428-436
2004
Homo sapiens
Manually annotated by BRENDA team
Lesner, A.; Wysocka, M.; Guzow, K.; Wiczk, W.; Legowska, A.; Rolka, K.
Development of sensitive cathepsin G fluorogenic substrate using combinatorial chemistry methods
Anal. Biochem.
375
306-312
2008
Homo sapiens
Manually annotated by BRENDA team
Korkmaz, B.; Moreau, T.; Gauthier, F.
Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
Biochimie
90
227-242
2008
Homo sapiens, Homo sapiens (P08311)
Manually annotated by BRENDA team
Burster, T.; Beck, A.; Poeschel, S.; Oren, A.; Baechle, D.; Reich, M.; Roetzschke, O.; Falk, K.; Boehm, B.O.; Youssef, S.; Kalbacher, H.; Overkleeft, H.; Tolosa, E.; Driessen, C.
Interferon-gamma regulates cathepsin G activity in microglia-derived lysosomes and controls the proteolytic processing of myelin basic protein in vitro
Immunology
121
82-93
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Campbell, E.J.; Owen, C.A.
The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
J. Biol. Chem.
282
14645-14654
2007
Homo sapiens
Manually annotated by BRENDA team
Rykl, J.; Thiemann, J.; Kurzawski, S.; Pohl, T.; Gobom, J.; Zidek, W.; Schlueter, H.
Renal cathepsin G and angiotensin II generation
J. Hypertens.
24
1797-1807
2006
Homo sapiens (P08311), Sus scrofa (Q95284), Sus scrofa
Manually annotated by BRENDA team
Lim, J.K.; Lu, W.; Hartley, O.; DeVico, A.L.
N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
J. Leukoc. Biol.
80
1395-1404
2006
Homo sapiens
Manually annotated by BRENDA team
Wysocka, M.; Legowska, A.; Bulak, E.; Jaskiewicz, A.; Miecznikowska, H.; Lesner, A.; Rolka, K.
New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P1 selected by combinatorial chemistry methods
Mol. Divers.
11
93-99
2007
Homo sapiens
Manually annotated by BRENDA team
Miyata, J.; Tani, K.; Sato, K.; Otsuka, S.; Urata, T.; Lkhagvaa, B.; Furukawa, C.; Sano, N.; Sone, S.
Cathepsin G: the significance in rheumatoid arthritis as a monocyte chemoattractant
Rheumatol. Int.
27
375-382
2007
Homo sapiens
Manually annotated by BRENDA team
Gale, A.J.; Rozenshteyn, D.
Cathepsin G, a leukocyte protease, activates coagulation factor VIII
Thromb. Haemost.
99
44-51
2008
Homo sapiens
Manually annotated by BRENDA team
Peterszegi, G.; Texier, S.; Robert, A.M.; Moulias, R.; Robert, L.
Increased elastase and cathepsin G activity in activated lymphocytes from aged patients Role of denutrition and dementia
Arch. Gerontol. Geriatr.
25
285-298
2008
Homo sapiens
Manually annotated by BRENDA team
Sienczyk, M.; Lesner, A.; Wysocka, M.; Legowska, A.; Pietrusewicz, E.; Rolka, K.; Oleksyszyn, J.
New potent cathepsin G phosphonate inhibitors
Bioorg. Med. Chem.
16
8863-8867
2008
Homo sapiens
Manually annotated by BRENDA team
Wilson, T.J.; Nannuru, K.C.; Singh, R.K.
Cathepsin G recruits osteoclast precursors via proteolytic activation of protease-activated receptor-1
Cancer Res.
69
3188-3195
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Stoeckle, C.; Sommandas, V.; Adamopoulou, E.; Belisle, K.; Schiekofer, S.; Melms, A.; Weber, E.; Driessen, C.; Boehm, B.O.; Tolosa, E.; Burster, T.
Cathepsin G is differentially expressed in primary human antigen-presenting cells
Cell. Immunol.
255
41-45
2009
Homo sapiens
Manually annotated by BRENDA team
Mambole, A.; Baruch, D.; Nusbaum, P.; Bigot, S.; Suzuki, M.; Lesavre, P.; Fukuda, M.; Halbwachs-Mecarelli, L.
The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase
J. Biol. Chem.
283
23627-23635
2008
Homo sapiens (P08311)
Manually annotated by BRENDA team
Korkmaz, B.; Attucci, S.; Juliano, M.A.; Kalupov, T.; Jourdan, M.L.; Juliano, L.; Gauthier, F.
Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
Nat. Protoc.
3
991-1000
2008
Homo sapiens
Manually annotated by BRENDA team
Dabek, M.; Ferrier, L.; Roka, R.; Gecse, K.; Annahazi, A.; Moreau, J.; Escourrou, J.; Cartier, C.; Chaumaz, G.; Leveque, M.; Ait-Belgnaoui, A.; Wittmann, T.; Theodorou, V.; Bueno, L.
Luminal cathepsin g and protease-activated receptor 4: a duet involved in alterations of the colonic epithelial barrier in ulcerative colitis
Am. J. Pathol.
175
207-214
2009
Homo sapiens
Manually annotated by BRENDA team
Burster, T.; Macmillan, H.; Hou, T.; Schilling, J.; Truong, P.; Boehm, B.O.; Zou, F.; Lau, K.; Strohman, M.; Schaffert, S.; Busch, R.; Mellins, E.D.
Masking of a cathepsin G cleavage site in vivo contributes to the proteolytic resistance of major histocompatibility complex class II molecules
Immunology
130
436-46
2010
Homo sapiens
Manually annotated by BRENDA team
Tausch, L.; Henkel, A.; Siemoneit, U.; Poeckel, D.; Kather, N.; Franke, L.; Hofmann, B.; Schneider, G.; Angioni, C.; Geisslinger, G.; Skarke, C.; Holtmeier, W.; Beckhaus, T.; Karas, M.; Jauch, J.; Werz, O.
Identification of human cathepsin G as a functional target of boswellic acids from the anti-inflammatory remedy frankincense
J. Immunol.
183
3433-3442
2009
Homo sapiens, Homo sapiens (P08311)
Manually annotated by BRENDA team
Kudo, T.; Kigoshi, H.; Hagiwara, T.; Takino, T.; Yamazaki, M.; Yui, S.
Cathepsin G, a neutrophil protease, induces compact cell-cell adhesion in MCF-7 human breast cancer cells
Mediators Inflamm.
2009
850940
2009
Homo sapiens
Manually annotated by BRENDA team
Reich, M.; Lesner, A.; Legowska, A.; Sienczyk, M.; Oleksyszyn, J.; Boehm, B.O.; Burster, T.
Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells
Mol. Immunol.
46
2994-2999
2009
Homo sapiens
Manually annotated by BRENDA team
Burster, T.; Macmillan, H.; Hou, T.; Boehm, B.O.; Mellins, E.D.
Cathepsin G: roles in antigen presentation and beyond
Mol. Immunol.
47
658-665
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Korkmaz, B.; Jegot, G.; Lau, L.C.; Thorpe, M.; Pitois, E.; Juliano, L.; Walls, A.F.; Hellman, L.; Gauthier, F.
Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates
FEBS J.
278
2635-2646
2011
Homo sapiens, Homo sapiens (P08311)
Manually annotated by BRENDA team
Raymond, W.W.; Trivedi, N.N.; Makarova, A.; Ray, M.; Craik, C.S.; Caughey, G.H.
How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution
J. Immunol.
185
5360-5368
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Siao, S.C.; Li, K.J.; Hsieh, S.C.; Wu, C.H.; Lu, M.C.; Tsai, C.Y.; Yu, C.L.
Tamm-Horsfall glycoprotein enhances PMN phagocytosis by binding to cell surface-expressed lactoferrin and cathepsin G that activates MAP kinase pathway
Molecules
16
2119-2134
2011
Homo sapiens
Manually annotated by BRENDA team
Zou, F.; Schaefer, N.; Palesch, D.; Bruecken, R.; Beck, A.; Sienczyk, M.; Kalbacher, H.; Sun, Z.; Boehm, B.O.; Burster, T.
Regulation of cathepsin G reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients
PLoS ONE
6
e22815
2011
Homo sapiens
Manually annotated by BRENDA team
Perrin, J.; Lecompte, T.; Tournier, A.; Morlon, L.; Marchand-Arvier, M.; Vigneron, C.
In vitro effects of human neutrophil cathepsin G on thrombin generation: Both acceleration and decreased potential
Thromb. Haemost.
104
514-522
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Sjoeberg, S.; Tang, T.T.; Ooerni, K.; Wu, W.; Liu, C.; Secco, B.; Tia, V.; Sukhova, G.K.; Fernandes, C.; Lesner, A.; Kovanen, P.T.; Libby, P.; Cheng, X.; Shi, G.P.
Cathepsin G activity lowers plasma LDL and reduces atherosclerosis
Biochim. Biophys. Acta
1842
2174-2183
2014
Homo sapiens, Homo sapiens (P08311), Mus musculus (P28293)
Manually annotated by BRENDA team
Cohen-Mazor, M.; Mazor, R.; Kristal, B.; Sela, S.
Elastase and cathepsin G from primed leukocytes cleave vascular endothelial cadherin in hemodialysis patients
BioMed Res. Int.
2014
459640
2014
Homo sapiens, Homo sapiens (P08311)
Manually annotated by BRENDA team
Woloszynek, J.C.; Hu, Y.; Pham, C.T.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions
J. Biol. Chem.
287
34101-34109
2012
Homo sapiens (P08311)
Manually annotated by BRENDA team
Faraday, N.; Schunke, K.; Saleem, S.; Fu, J.; Wang, B.; Zhang, J.; Morrell, C.; Dore, S.
Cathepsin G-dependent modulation of platelet thrombus formation in vivo by blood neutrophils
PLoS ONE
8
e71447
2013
Homo sapiens, Homo sapiens (P08311), Mus musculus, Mus musculus (P28293)
Manually annotated by BRENDA team
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