Information on EC 3.4.23.3 - gastricsin

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY hide
3.4.23.3
-
RECOMMENDED NAME
GeneOntology No.
gastricsin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
more restricted specificity than pepsin A, but shows preferential cleavage at Tyr-/- bonds. High activity on hemoglobin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
9012-71-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pepsin C-1 and C-2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the major useful function of progastricsin (PGC) includes production of pro-antimicrobial substance in seminal plasma. The action of PGC in the stomach is to degrade dietary proteins. However, in seminal fluid, it activates defensins for local antimicrobial defense. On the other hand, intracellular proprotein activation by PGC in acidic organelle, such as in proSP-B proteolysis, is important on the processing in the secretory pathway of alveolar type-2 cells
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Ala-Leu-Val-His-NH2 + H2O
?
show the reaction diagram
-
very low activity
-
-
?
acetyl-Ala-Leu-Val-His-OH + H2O
?
show the reaction diagram
-
very low activity
-
-
?
acetyl-Ala-Phe-Leu-Val-His-NH2 + H2O
?
show the reaction diagram
acetyl-Phe-Leu-Val-His methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Leu-Val-His-NH2 + H2O
?
show the reaction diagram
acetyl-Tyr-Leu-Val-His methyl ester + H2O
?
show the reaction diagram
acetyl-Tyr-Leu-Val-His-NH2 + H2O
?
show the reaction diagram
acetyl-Tyr-Leu-Val-His-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Albumin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
insulin B chain + H2O
?
show the reaction diagram
-
cleavage of sites Leu15-Tyr16 and Tyr16-Leu17
-
-
?
Leu-Ser-(4-nitro)Phe-norleucine-Ala-Leu methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
?
show the reaction diagram
oxidized insulin B chain + H2O
?
show the reaction diagram
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
-
-
?
Pro-Thr-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
reduced and carboxymethylated ribonuclease A + H2O
?
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
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-(p-nitrophenoxy)propane
-
-
1,2-epoxy-3-(p-nitrophenoxy)propane
-
-
Acetyl-Phe
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hydrolysis of acetyl-Phe-Leu-Val-His-amide
alpha2-Macroglobulin
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activity with reduced and carboxymethylated ribonuclease A is significantly inhibited, activity with oxidized insulin B-chain is scarcely inhibited
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Diazoacetyl-DL-norleucine methyl ester
isovaleryl pepstatin
-
-
-
L-363,564
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a statyl peptide based on renin substrate angiotensinogen
L-364099
-
-
-
Lactoyl-pepstatin
-
very weakly
-
p-bromophenylacyl bromide
-
-
Pepstatin
pepstatin A
-
-
[1S-(1R*,2R*,3S*)]-[N-(4-morpholinylsulfonyl)-L-phenylalanyl]-N-[1-(cyclohexylmethyl)-2,3-dihydroxy-5-methylhexyl]-4,5-didehydro-L-norvalinamide
-
-
-
[1S-(1R*,2R*,4S*)]-[N-(4-morpholinylsulfonyl)-L-phenylalanyl]-N-[1-(cyclohexylmethyl)-2,4-dihydroxy-5-methylhexyl]-4,5-didehydro-L-norvalinamide
-
-
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[1S-[1R*[R*(R*)],2R*,4S*]]-[N-(4-morpholinylsulfonyl)-L-phenylalanyl]-N-[1-(cyclohexylmethyl)-2,4-dihydroxyhexyl]-N6-[(methylamino)thioxomethyl]-L-lysinamide
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-
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additional information
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the pepsin C activity decreases due to its autocatalytical activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.51 - 0.7
acetyl-Ala-Phe-Leu-Val-His-NH2
1.84
acetyl-Phe-Leu-Val-His methyl ester
2.76
acetyl-Phe-Leu-Val-His-NH2
-
-
0.28 - 1.71
acetyl-Tyr-Leu-Val-His methyl ester
0.82 - 4.31
acetyl-Tyr-Leu-Val-His-NH2
0.098 - 0.42
Pro-Thr-Glu-Phe-(NO2)Phe-Arg-Leu
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 7.01
acetyl-Ala-Phe-Leu-Val-His-NH2
5.13
acetyl-Phe-Leu-Val-His methyl ester
Sus scrofa
-
-
0.6 - 6.12
acetyl-Phe-Leu-Val-His-NH2
1.06 - 5.76
acetyl-Tyr-Leu-Val-His methyl ester
1.07 - 4.45
acetyl-Tyr-Leu-Val-His-NH2
55
Pro-Thr-Glu-Phe-(NO2)Phe-Arg-Leu
Sus scrofa
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 3
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hemoglobin
5
-
assay at
additional information
-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1 - 4
-
pH 1.1: about 60% of maximal activity, pH 4.0: about 35% of maximal activity
1.2 - 3.5
-
pH 1.2: about 75% of maximal activity, pH 3.5: about 55% of maximal activity
1.3 - 4.5
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pH 1.3: about 75% of maximal activity, pH 4.5: about 35% of maximal activity, pepsin C-2
1.4 - 4.5
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pH 1.4: about 90% of maximal activity, pH 4.5: about 40% of maximal activity, pepsin C-1
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
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calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is produced by mammary carcinomas and cysts, but not by the normal resting mammary gland
Manually annotated by BRENDA team
-
pepsinogen C transcript is first detected at 41 days post hatching and continuously expressed through to adult fish
Manually annotated by BRENDA team
-
pepsinogen C transcript is first detected at 41 days post hatching and continuously expressed through to adult fish
Manually annotated by BRENDA team
-
pepsinogen C transcript is first detected at 41 days post hatching and continuously expressed through to adult fish
Manually annotated by BRENDA team
-
pepsinogen C transcript is first detected at 41 days post hatching and continuously expressed through to adult fish
Manually annotated by BRENDA team
additional information
-
no expression in healthy breast tissue, reabsorption of zymogen from serum into kidney
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
the MW of pepsinogen C is 35000 Da, gel filtration
32800
-
gel filtration
35460
-
calculation from nucleotide sequence; electrospray mass spectrometry
41400
-
calculation from amino acid composition
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
contains no carbohydrate
proteolytic modification
side-chain modification
-
pepsinogen C-2 contains an Asn-linked carbohydrate chain of about 2000 Da
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure determination
-
molecular structure and comparison with that of porcine pepsinogen
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the pepsin C activity decreases due to its autocatalytical activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from stomach
-
native zymogen
native zymogen from stomach, prostate, breast cysts fluid, and seminal plasma, native mature enzyme from gastric fluid by anion exchange chromatography
-
pepsinogen C-1 and C-2
-
pepsinogen C1- and C-2
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rapid single-step separation of pepsin from gastricsin from crude human gastric juice and prepurified gastric mucosa extract
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination
-
location on chromosome 6
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
progasticsin gene expression is up-regulated following gastrin, secretin, and forskolin stimulation of adenylate cyclase activity
the decrease of progastricsin expression indicates dedifferentiation or malignancy of cancer cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine