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Information on EC 3.4.23.3 - gastricsin and Organism(s) Homo sapiens and UniProt Accession P20142

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.3 gastricsin
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P20142 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
more restricted specificity than pepsin A, but shows preferential cleavage at Tyr-/- bonds. High activity on hemoglobin
Synonyms
EC 3.4.4.22, More, parapepsin II, pepsin C, pepsin II, pepsinogen C, PGC, pig parapepsin II, progastricsin, seminal pepsin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pepsin C
pepsin II
247
-
pepsinogen C
295254
-
PGC
295254
-
pig parapepsin II
-
-
-
-
progastricsin
295254
-
seminal pepsin
247
-
additional information
247
the enzyme belongs to the A1 peptidase family
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
acid endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9012-71-9
-
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-Phe-Leu-Val-His-NH2 + 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
-
-
-
-
?
Albumin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + 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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha2-Macroglobulin
-
activity with reduced and carboxymethylated ribonuclease A is significantly inhibited, activity with oxidized insulin B-chain is scarcely inhibited
-
isovaleryl pepstatin
-
-
-
L-363,564
-
a statyl peptide based on renin substrate angiotensinogen
L-364099
-
-
Lactoyl-pepstatin
-
very weakly
-
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
-
-
[1S-[1R*[R*(R*)],2R*,4S*]]-[N-(4-morpholinylsulfonyl)-L-phenylalanyl]-N-[1-(cyclohexylmethyl)-2,4-dihydroxyhexyl]-N6-[(methylamino)thioxomethyl]-L-lysinamide
-
-
additional information
-
the pepsin C activity decreases due to its autocatalytical activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.51
acetyl-Ala-Phe-Leu-Val-His-NH2
-
-
2.76
acetyl-Phe-Leu-Val-His-NH2
-
-
0.42
Pro-Thr-Glu-Phe-(NO2)Phe-Arg-Leu
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
acetyl-Ala-Phe-Leu-Val-His-NH2
-
-
0.6
acetyl-Phe-Leu-Val-His-NH2
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
assay at
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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
-
synthesis
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
-
in gastric juice, vaginal fluid, serum, and seminal plasma, no secretion in urine
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PEPC_HUMAN
388
0
42426
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, calculated from amino acid sequence
35460
-
calculation from nucleotide sequence; electrospray mass spectrometry
additional information
-
amino acid sequence, 24 residues, near the amino terminus
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, calculated from amino acid sequence
additional information
-
secondary and tertiary structure determination
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure determination
-
molecular structure and comparison with that of porcine pepsinogen
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the pepsin C activity decreases due to its autocatalytical activity
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
native zymogen from stomach, prostate, breast cysts fluid, and seminal plasma, native mature enzyme from gastric fluid by anion exchange chromatography
-
rapid single-step separation of pepsin from gastricsin from crude human gastric juice and prepurified gastric mucosa extract
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
location on chromosome 6
-
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
the tissue expression of progatricsin represents a powerful tool for the diagnosis of prostate cancer. The enzyme is also a biomarker for gastric carcinoma and plays a direct role in the development of breast tumor progression
medicine
-
potential interest as a biochemical marker of the hormonal imbalance underlying these pathologies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jones, A.T.; Green, B.N.; Wood, S.P.; Roberts, N.B.
The amino terminal sequences of acid proteases-human pepsin and gastricsin and the protease of Rhizopus chinensis
Aspartic Proteinases: Structure, Function, Biology and Biomedical Implications (Takahashi, K. , ed. ), Plenum Press, New York
83-89
1995
Homo sapiens
Manually annotated by BRENDA team
James, M.; Moore, S.; Sielecki, A.; Chernaia, M.; Tarasova, N.
Pepsinogens and pepsins from house musk shrew, Suncus murinus: purification, characterization, determination of the amino-acid sequences of the activation segments, and analysis of proteolytic specificities
Aspartic Proteinases: Structure, Function, Biology and Biomedical Implications (Takahashi, K. , ed. ), Plenum Press, New York
11-18
1995
Homo sapiens
Manually annotated by BRENDA team
Sepulveda, P.; Jackson, K.W.; Tang, J.
Identification of the acid proteinase in human seminal fluid as a gastricsin originating in the prostate
Biochem. Biophys. Res. Commun.
63
1106-1112
1975
Homo sapiens
Manually annotated by BRENDA team
Reid, W.A.; Vongsorasak, L.; Svasti, J.; Valler, M.J.; Kay, J.
X-ray studies of aspartic proteinase-statine inhibitor complexes
Cell Tissue Res.
236
597-600
1984
Homo sapiens
Manually annotated by BRENDA team
Chiang, L.; Contreras, L.; Chiang, J.; Ward, P.H.
Primary structure and transcriptional regulation of rat pepsinogen C gene
Arch. Biochem. Biophys.
210
14-20
1981
Homo sapiens
Manually annotated by BRENDA team
Cooper, J.B.; Foundling, S.I.; Blundell, T.L.; Boger, J.; Jupp, R.A.; Kay, J.
Separation of human pepsin and gastricsin by affinity chromatography with an immobilized synthetic inhibitor
Biochemistry
28
8596-8603
1989
Homo sapiens
Manually annotated by BRENDA team
Kucerova, Z.; Pohl, J.; Korbova, L.
Purification and characterization of bovine gastricsin
J. Chromatogr.
376
409-412
1986
Homo sapiens
Manually annotated by BRENDA team
Ryle, A.P.; Auffret, C.A.
The specificity of some pig and human pepsins towards synthetic peptide substrates
Biochem. J.
179
247-249
1979
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Richmond, V.; Tang, J.; Wolf, S.; Trucco, R.E.; Caputto, R.
Chromatographic isolation of gastricsin, the proteolytic enzyme from gastric juice with pH optimum 3.2
Biochim. Biophys. Acta
29
453-454
1958
Homo sapiens
Manually annotated by BRENDA team
Sanchez, L.M.; Freije, J.P.; Merino, A.M.; Vizoso, F.; Foltmann, B.; Lopez-Otin, C.
Separation of porcine pepsinogen A and progastricsin. Sequencing of the first 73 amino acid residues in progastricsin
J. Biol. Chem.
267
24725-24731
1992
Homo sapiens
Manually annotated by BRENDA team
Hayano, T.; Sogawa, K.; Ichihara, Y.; Fujii-Kuriyama, Y.; Takahashi, K.
Gastricsin-mediated proteolytic degradation of human seminal fluid proteins at pH levels found in the human vagina
J. Biol. Chem.
263
1382-1385
1988
Homo sapiens
Manually annotated by BRENDA team
Szecsi, P.B.; Lilja, H.
Pepsinogen C and pepsin C from gastric mucosa of Japanese monkey. Purification and characterization
J. Androl.
14
351-358
1993
Homo sapiens
Manually annotated by BRENDA team
Rao, C.M.; Scarborough, P.E.; Kay, J.; Batley, B.; Rapundalo, S.; Klutchko, S.; Taylor, M.D.; Lunney, E.A.; Humblet, C.C.; Dunn, B.M.
Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variation
J. Med. Chem.
36
2614-2620
1993
Homo sapiens
Manually annotated by BRENDA team
Taggart, R.T.; Cass, L.G.; Mohandas, P.; Derby, P.J.; Barr, P.J.; Pals, G.; Bell, G.
Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A
J. Biol. Chem.
264
375-379
1989
Homo sapiens
Manually annotated by BRENDA team
Athauda, S.B.; Nishigai, M.; Arakawa, H.; Ikai, A.; Ukai, M.; Takahashi, K.
Inhibition of human pepsin and gastricsin by alpha2-macroglobulin
J. Enzyme Inhib. Med. Chem.
18
219-224
2003
Homo sapiens
Manually annotated by BRENDA team
Schreiber, S.; Buecker, R.; Groll, C.; Azevedo-Vethacke, M.; Scheid, P.; Gatermann, S.; Josenhans, C.; Suerbaum, S.
Gastric antibacterial efficiency is different for pepsin A and C
Arch. Microbiol.
184
335-340
2006
Homo sapiens
Manually annotated by BRENDA team
Tang, J.
Gastricsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
38-43
2004
Homo sapiens, Macaca fuscata, Sus scrofa, Xenopus laevis
-
Manually annotated by BRENDA team
Filuszova, M.; Kucerova, Z.; Ticha, M.
Peptide inhibitor modified magnetic particles for pepsin separation
J. Sep. Sci.
32
2017-2021
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hassan, M.; Toor, A.; Ahmad, F.
Progastriscin: Structure, function, and its role in tumor progression
J. Mol. Cell Biol.
2
118-127
2010
Homo sapiens, Homo sapiens (P20142)
Manually annotated by BRENDA team
Foltz, E.; Azad, S.; Everett, M.L.; Holzknecht, Z.E.; Sanders, N.L.; Thompson, J.W.; Dubois, L.G.; Parker, W.; Keshavjee, S.; Palmer, S.M.; Davis, R.D.; Lin, S.S.
An assessment of human gastric fluid composition as a function of PPI usage
Physiol. Rep.
3
0000
2015
Homo sapiens
Manually annotated by BRENDA team
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