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Information on EC 3.4.21.36 - pancreatic elastase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.36 pancreatic elastase
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-/-
Synonyms
pancreatic elastase, elastase 1, elastase-1, cela1, serine elastase, pancreatic elastase-1, cela3b, chymotrypsin-like elastase, prt-201, cela3a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CELA3A
-
isoform
CELA3B
-
isoform
chymotrypsin-like elastase
-
-
elastase
-
-
-
-
elastase-1
-
-
elaszym
-
-
-
-
pancreatic elastase 3
-
-
pancreatic elastase 3B
-
pancreatic elastase I
-
-
-
-
pancreatic elastase-1
-
-
pancreatopeptidase E
-
-
-
-
PE-1
-
-
peptidase, pancreato-, E
-
-
-
-
PRT-201
serine elastase
-
-
-
-
type I pancreatic elastase
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
848900-32-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-p-nitrophenylester + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha1-antitrypsin
-
-
-
alpha2-Macroglobulin
-
-
-
elafin
-
-
-
NaCl
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
phenylmethanesulfonyl fluoride
-
-
Schistocerca gregaria proteinase inhibitor 2 variant E1
-
Tyr-Cys-Thr-Leu-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E10
-
Ala-Cys-Thr-Leu-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E11
-
Ala-Cys-Thr-Leu-Met-Tyr-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E12
-
Tyr-Cys-Thr-Leu-Met-Leu-Cys-Ala
-
Schistocerca gregaria proteinase inhibitor 2 variant E2
-
Tyr-Cys-Thr-Ile-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E3
-
Tyr-Cys-Thr-Val-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E4
-
Tyr-Cys-Thr-Met-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E5
-
Tyr-Cys-Thr-Ala-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E6
-
Tyr-Cys-Thr-Ser-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E7
-
Tyr-Cys-Thr-Ile-Met-Glu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E8
-
Tyr-Cys-Thr-Leu-Arg-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E9
-
Tyr-Cys-Thr-Leu-Met-Tyr-Cys-His
-
trappin-2
-
-
-
additional information
-
serum from normal volunteers and patients with alpha 1-antitrypsin deficiency completely inactivate PRT-201 elastase activity in vitro
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trypsin
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.374 - 1.089
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
0.484 - 1.06
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
0.259 - 0.722
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
0.288 - 0.452
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
0.984 - 1.447
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
0.43 - 1.178
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
0.513
tert-butyloxycarbonyl-Ala-p-nitrophenylester
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.9 - 24.8
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
0.99 - 1.25
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
1.01 - 1.16
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
0.24
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
0.14 - 0.26
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
2.44 - 3.66
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21 - 66
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
0.93 - 2.6
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
1.6 - 3.9
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
0.53 - 0.83
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
0.099 - 0.26
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
2.1 - 8.5
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000075
elafin
-
panreatic elastase
-
0.00000032
trappin-2
-
pancreatic elastase
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.2
-
50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
assay at
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?
CELA1_HUMAN
258
0
27798
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26300
-
x * 26300, SDS-PAGE
30000
-
gel filtration
30790
-
amino acid analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 26300, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
no carbohydrate
side-chain modification
-
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
-
29635
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis, unstable
-
dilute solutions, stable
-
freezing and thawing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 6.5, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
fecal elastase-1 concentrations correlates negatively with age and are significantly lower among subjects over 70 years old compared to controls
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mallory, P.A.; Travis, J.
Human pancreatic enzymes: purification and characterization of a nonelastolytic enzyme, protease E. resembling elastase
Biochemistry
14
722-730
1975
Homo sapiens
Manually annotated by BRENDA team
Fujimoto, K.; Ogawa, M.; Saito, N.; Kosaki, G.; Minamiura, N.; Yamamoto, T.
A novel method of isolation and some characteristic properties of human pancreatic elastases
Biochim. Biophys. Acta
612
262-267
1980
Homo sapiens
Manually annotated by BRENDA team
Ohlsson, K.; Olsson, A.S.
Purification and partial characterization of human pancreatic elastase
Hoppe-Seyler's Z. Physiol. Chem.
357
1153-1161
1976
Homo sapiens
Manually annotated by BRENDA team
Largman, C.; Brodrick, J.W.; Geokas, M.C.
Purification and characterization of two human pancreatic elastases
Biochemistry
15
2491-2500
1976
Homo sapiens
Manually annotated by BRENDA team
Wendorf, P.; Linder, D.; Sziegoleit, A.; Geyer, R.
Carbohydrate structure of human pancreatic elastase 1
Biochem. J.
278
505-514
1991
Homo sapiens
Manually annotated by BRENDA team
Wendorf, P.; Geyer, R.; Sziegoleit, A.; Linder, D.
Localization and characterization of the glycosylation site of human pancreatic elastase 1
FEBS Lett.
249
275-278
1989
Homo sapiens
Manually annotated by BRENDA team
Zani, M.L.; Nobar, S.M.; Lacour, S.A.; Lemoine, S.; Boudier, C.; Bieth, J.G.; Moreau, T.
Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris
Eur. J. Biochem.
271
2370-2378
2004
Homo sapiens
Manually annotated by BRENDA team
Walkowiak, J.; Wadolowska, L.; Szaflarska-Poplawska, A.; Lisowska, A.; Bugajewska, A.; Przyslawski, J.
The elimination of meat from the diet selectively decreases pancreatic elastase secretion
Br. J. Nutr.
98
154-158
2007
Homo sapiens
Manually annotated by BRENDA team
Chen, C.Y.; Tsai, W.L.; Wu, H.C.; Syu, M.J.; Wu, C.C.; Shiesh, S.C.
Diagnostic role of biliary pancreatic elastase for cholangiocarcinoma in patients with cholestasis
Clin. Chim. Acta
390
82-89
2008
Homo sapiens (Q9UNI1), Homo sapiens
Manually annotated by BRENDA team
Naruse, S.; Ishiguro, H.; Ko, S.B.; Yoshikawa, T.; Yamamoto, T.; Yamamoto, A.; Futakuchi, S.; Goto, H.; Saito, Y.; Takahashi, S.
Fecal pancreatic elastase: a reproducible marker for severe exocrine pancreatic insufficiency
J. Gastroenterol.
41
901-908
2006
Homo sapiens
Manually annotated by BRENDA team
Benahmed, N.A.; Manene, D.; Barbot, L.; Kapel, N.
Fecal pancreatic elastase in infants under 2 years of age
Ann. Biol. Clin. (Paris)
66
549-552
2008
Homo sapiens
Manually annotated by BRENDA team
Erickson, J.A.; Aldeen, W.E.; Grenache, D.G.; Ashwood, E.R.
Evaluation of a fecal pancreatic elastase-1 enzyme-linked immunosorbent assay: Assessment versus an established assay and implication in classifying pancreatic function
Clin. Chim. Acta
397
87-91
2008
Homo sapiens
Manually annotated by BRENDA team
Herzig, K.; Purhonen, A.; Rsnen, K.; Idziak, J.; Juvonen, P.; Phillps, R.; Walkowiak, J.
Fecal pancreatic elastase-1 levels in older individuals without known gastrointestinal diseases or diabetes mellitus
BMC Geriatr.
11
4-4
2011
Homo sapiens
Manually annotated by BRENDA team
Qamar, A.A.; Burke, S.K.; Lafleur, J.D.; Ding, B.C.; Bland, K.S.; Wong, M.D.; Gustafson, P.N.; Blair, A.T.; Franano, F.N.
The ability of serum from alpha 1-antitrypsin-deficient patients to inhibit PRT-201, a recombinant human type I pancreatic elastase
Biotechnol. Appl. Biochem.
59
22-28
2012
Homo sapiens
Manually annotated by BRENDA team
Burke, S.K.; Macdonald, K.; Moss, E.; Bunton, D.; Starcher, B.; Wong, M.D.; Bland, K.S.; Franano, F.N.
Effects of recombinant human type I pancreatic elastase on human atherosclerotic arteries
J. Cardiovasc. Pharmacol.
64
530-535
2014
Homo sapiens
Manually annotated by BRENDA team
Boros, E.; Szabo, A.; Zboray, K.; Heja, D.; Pal, G.; Sahin-Toth, M.
Overlapping specificity of duplicated human pancreatic elastase 3 isoforms and archetypal porcine elastase 1 provides clues to evolution of digestive enzymes
J. Biol. Chem.
292
2690-2702
2017
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team