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Information on EC 3.4.23.1 - pepsin A and Organism(s) Homo sapiens

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.1 pepsin A
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This record set is specific for:
Homo sapiens
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-/-Val, Gln4-/-His, Glu13-/-Ala, Ala14-/-Leu, Leu15-/-Tyr, Tyr16-/-Leu, Gly23-/-Phe, Phe24-/-Phe and Phe25-/-Tyr bonds in the B chain of insulin
Synonyms
pepsin, pepsinogen a, pepsin a, pepsin 1, shewasin d, pepsin a2, pg1-1, pg2-2, pep/pag-l, pepsins a1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elixir lactate of pepsin
-
-
-
-
fundus-pepsin
-
-
-
-
lactated pepsin
-
-
-
-
lactated pepsin elixir
-
-
-
-
P I
-
-
-
-
pepsin
pepsin A
-
-
pepsin D
-
-
-
-
pepsin fortior
-
-
-
-
Pepsin I/II
-
-
-
-
pepsin R
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-75-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AFPLEFEREL + H2O
AFPLEF + EREL
show the reaction diagram
-
-
-
-
?
AFPLEFFREL + H2O
AFPLEF + FREL
show the reaction diagram
-
-
-
-
?
AFPLEFIREL + H2O
AFPLEF + IREL
show the reaction diagram
-
-
-
-
?
dynorphin A (1-7) + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
HPHLSFMAI + H2O
HPHLSF + Met-Ala-Ile + ?
show the reaction diagram
-
best substrate
-
-
?
KPAEFFRL + H2O
KPAEF + FRL
show the reaction diagram
-
-
-
-
?
KYSSWYVAL + H2O
KYSSW + YVAL
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
NT/NMN (142-151) + H2O
KIPYIL + KRQL
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
-
-
?
POMC (165-174) + H2O
AFPLE + FKREL
show the reaction diagram
-
-
-
-
?
Ribonuclease + H2O
?
show the reaction diagram
-
reduced and carboxymethylated ribonuclease A
-
?
serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
substance P + H2O
RPKPQQF + FGLM
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
alpha2-Macroglobulin
-
activity towards reduced and carboxymethylated ribonuclease A is significantly inhibited at pH 5.5, the activity towards a peptide substrate, oxidized insulin B-chain, is scarcely inhibited
-
Diazoacetyl-DL-norleucine methyl ester
-
presence of Cu2+
p-bromophenylacyl bromide
-
-
pepstatin
-
-
pepstatin A
-
-
Val-D-Leu-Pro-Phe-Phe-Val-D-Leu
additional information
-
diazoketones
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
AFPLEFEREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
0.084
AFPLEFFREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
0.079
AFPLEFIREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
0.029
POMC (165-174)
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.9
AFPLEFEREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
85
AFPLEFFREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
56
AFPLEFIREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
2.7
POMC (165-174)
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
AFPLEFEREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
1000
AFPLEFFREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
730
AFPLEFIREL
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
93
POMC (165-174)
-
in 0.2 M sodium formate buffer, pH 4.0, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 5
-
with serum albumin as a substrate, the enzyme retains 70% of its activity at pH 4.0 and almost 40% at pH 5.0
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
42
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
secretions from the trachea, lung, nose, sinus, middle ear, and exhaled breath condensate
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PEPA3_HUMAN
388
0
41976
Swiss-Prot
Secretory Pathway (Reliability: 3)
PEPA4_HUMAN
388
0
41977
Swiss-Prot
Secretory Pathway (Reliability: 3)
PEPA5_HUMAN
388
0
41993
Swiss-Prot
Secretory Pathway (Reliability: 3)
B7ZW10_HUMAN
388
0
42021
TrEMBL
Secretory Pathway (Reliability: 3)
B7ZW16_HUMAN
388
0
41991
TrEMBL
Secretory Pathway (Reliability: 3)
B7ZW66_HUMAN
388
0
41993
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1S5UZ02_HUMAN
388
0
41977
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
gel filtration, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L291S
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
L291S/L298Q
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
L298Q
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
M289D
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
binding to immobilized inhibitor Val-D-Leu-Pro-Phe-Phe-Val-D-Leu
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the enzyme is a biomarker of gastric reflux into the esophagus, airways, and lungs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryle, A.P.
Pepsins, gastricsins and their zymogens
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
228-238
1984
Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Seijffers, M.J.; Miller, L.L.; Segal, H.L.
Partial characterization of human pepsin I, pepsin IIA, pepsin IIB, and pepsin III
Biochemistry
3
1203-1209
1964
Homo sapiens
Manually annotated by BRENDA team
Roberts, N.B.; Taylor, W.H.
The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose
Biochem. J.
169
607-615
1978
Homo sapiens
Manually annotated by BRENDA team
Pohl, J.; Zaoral, M.; Jindra, A.; Kostka, V.
Purification of pepsins and cathepsin D by affinity chromatography on Sepharose 4B with an immobilized synthetic inhibitor
Anal. Biochem.
139
265-271
1984
Gallus gallus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Athauda, S.B.P.; Tanji, M.; Kageyama, T.; Takahashi, K.
A comparative study on the NH2-terminal amino acid sequences and some other properties of six isozymic forms of human pepsinogens and pepsins
J. Biochem.
106
920-927
1989
Homo sapiens
Manually annotated by BRENDA team
Fujinaga, M.; Chernaia, M.M.; Tarasova, N.I.; Mosimann, S.C.; James, M.N.G.
Crystal structure of human pepsin and its complex with pepstatin
Protein Sci.
4
960-972
1995
Homo sapiens
Manually annotated by BRENDA team
Ruenwongsa, P.; Chulavatnatol, M.
Acidic protease from human seminal plasma. Purification and some properties of active enzyme and of proenzyme
J. Biol. Chem.
250
7574-7578
1975
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
Kageyama, T.
Role of S1 loop residues in the substrate specificities of pepsin A and chymosin
Biochemistry
43
15122-15130
2004
Homo sapiens
Manually annotated by BRENDA team
Kageyama, H.; Ueda, H.; Tezuka, T.; Ogasawara, A.; Narita, Y.; Kageyama, T.; Ichinose, M.
Differences in the P1' substrate specificities of pepsin A and chymosin
J. Biochem.
147
167-174
2010
Homo sapiens, Sus scrofa
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, Sus scrofa
Manually annotated by BRENDA team
Johnston, N.; Dettmar, P.W.; Ondrey, F.G.; Nanchal, R.; Lee, S.H.; Bock, J.M.
Pepsin biomarker, mediator, and therapeutic target for reflux and aspiration
Ann. N. Y. Acad. Sci.
1434
282-289
2018
Homo sapiens
Manually annotated by BRENDA team
Petersen, K.U.
Pepsin and its importance for functional dyspepsia relic, regulator or remedy?
Dig. Dis.
36
98-105
2018
Homo sapiens
Manually annotated by BRENDA team