Information on EC 3.4.21.20 - cathepsin G

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.20
-
RECOMMENDED NAME
GeneOntology No.
cathepsin G
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
specificity similar to chymotrypsin C
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
56645-49-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Balb/c mice
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-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
-
-
-
-
?
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-(4-pyridyl-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-pyridyl-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
-
-
?
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
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
low-density lipoprotein + H2O
?
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-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
serum amyloid P + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-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-alanyl-alanyl-prolyl-phenylalanyl-aminomethyl-coumarin + H2O
?
show the reaction diagram
-
a fluorogenic substrate
-
-
?
succinyl-Phe-Leu-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
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 SUBSTRATES
NATURAL PRODUCTS
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
angiotensinogen + H2O
angiotensin I + ?
show the reaction diagram
angiotensinogen + H2O
angiotensin II + ?
show the reaction diagram
cadherin + 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
low-density lipoprotein + H2O
?
show the reaction diagram
myelin basic protein + H2O
myelin basic protein peptide fragments
show the reaction diagram
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
-
-
?
serum amyloid P + H2O
?
show the reaction diagram
-
-
-
-
?
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-Antichymotrypsin
-
alpha1-CT
-
-
-
alpha1-protease inhibitor
-
-
-
Alpha1-proteinase inhibitor
-
alpha1alpha2-macroglobulin
-
-
-
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
-
-
-
Eglin c
furoylsaccharin
-
-
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-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-chloromethylketone
-
irreversible inhibitor
N-succinyl-L-Val-L-Pro-L-Phe(OPh)2
-
irreversible CatG inhibitor, complete inhibition at 0.01 mM
N-succinyl-L-Val-L-Pro-L-Phe-(OPh)2
-
irreversible inhibitor
N-tosyl-L-phenylalanine chloromethyl ketone
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
Na-tosyl-Phe-chloromethylketone
Pepstatin
-
15% inhibition after 30 min at 0.1 mM at 25°C
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
-
-
0.52
N-acetyl-L-phenylalanine-p-nitrophenyl ester
-
-
0.42 - 2.6
N-benzoyl-L-tyrosine ethyl ester
0.12 - 3.1
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
2.7 - 3.9
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
0.86
succinyl-Ala-Ala-Pro-Phe-p-nitroanilde
-
-
-
0.24
succinyl-Phe-Leu-Phe-p-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
Homo sapiens
-
pH 7.5, 25°C
0.421
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
pH 7.5, 25°C
6
methoxysuccinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide
Homo sapiens
-
-
16.5
methoxysuccinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitrophenylanilide
Rattus norvegicus
-
-
20.2 - 68.3
N-acetyl-L-phenylalanine-p-nitrophenyl ester
3
N-benzoyl-L-tyrosine ethyl ester
Homo sapiens
-
-
9 - 100
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
additional information
additional information
Homo sapiens
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2054
Abz-GIAPFCDLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168006
817
Abz-GIATFCDLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
144538
263
Abz-GIATFCMLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
144540
560
Abz-GIATFCPLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168013
68
Abz-GIATFCRLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
144541
175
Abz-GIATFDMLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168009
162
Abz-GIATFRMLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168010
217
Abz-GIATFSMLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168011
69
Abz-GIATFWMLMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168012
1700
Abz-GIEPFSDPMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168007
190
Abz-GIEPKSDPMPEQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168008
153.8
Abz-TPFSALQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168014
8.1
Abz-TPKSALQ-EDDnp
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168015
69
Abz-TPWSALQ-YNO2
Homo sapiens
-
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
168016
7.1 - 330
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
4450
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 - 2.48
Lys16-aprotinin
-
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
6.51
-
purified enzyme
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
-
-
8 - 8.5
-
-
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
6.6 - 8.4
-
pH 6.6: more than 50% of maximal activity, pH 8.4: optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
40
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
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
-
monocyte/macrophage 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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
-
gel filtration
23500
-
gel filtration
25500
-
x * 25500, SDS-PAGE
26000
-
MALDI-TOF
27000
-
x * 27000, SDS-PAGE
28400
-
1 * 28400, SDS-PAGE
28500
-
x * 28500
28900
-
calculated
29400
-
x * 29400, SDS-PAGE
30000
-
x * 30000, SDS-PAGE
39000
-
Western blot
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 28400, SDS-PAGE
additional information
MALDI-TOF mass spectrometrical peptide finger printing, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with the inhibitor JNJ-10311795, 1.85 A resolution
-
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
-
heparin-5 PW column chromatography and Mono S 5/5 HR column chromatography
-
native enzyme from kidney by anion exchange and hydroxyapatite chromatography, lentil lectin affinity chromatography, and gel filtration or chymostatin-antipain affinity chromatography, to homogeneity
Protein G Sepharose 4 Fast Flow
-
to homogeneity from leukocytes, 108.5fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 insect cells
-
the gene is located at chromosome 14q11.2
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
increased expression at the tumor-bone interface
-
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
up-regulated at the tumor-bone interface
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S189A/A226E
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme and develops Lys-thioesterase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a therapeutic target
medicine
pharmacology
-
structure-based drug design