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Information on EC 3.4.21.36 - pancreatic elastase and Organism(s) Homo sapiens and UniProt Accession Q9UNI1

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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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9UNI1 not found.
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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, pancreatic elastase i, prt-201, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pancreatic elastase 3B
-
CELA3A
-
isoform
CELA3B
-
isoform
chymotrypsin-like elastase
-
-
elastase
-
-
-
-
elastase-1
-
-
elaszym
-
-
-
-
pancreatic elastase 3
-
-
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
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-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
-
UniProt
Manually annotated by BRENDA team
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