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Information on EC 3.4.23.2 - pepsin B
for references in articles please use BRENDA:EC3.4.23.2
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.23 Aspartic endopeptidases
3.4.23.2 pepsin B
IUBMB Comments
Formed from pig pepsinogen B. In peptidase family A1 (pepsin A family)
The enzyme appears in viruses and cellular organisms
- 3.4.23.2
- pepsinogen
- zymogen
- chymosin
- proteinases
- progastricsin
- gelatin
- prosegment
- prochymosin
- juice
- gelatinase
- gastricsin
-
calf
- mucosa
-
immunoelectrophoresis
- food industry
Reaction Schemes
showdegradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe
Synonyms
pepsin b, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.4.2
-
-
formerly
-
gelatinase
-
-
-
-
parapepsin I
-
-
-
-
pepsin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe
degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe
mechanism, concerted action of different pepsins
-
degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-48-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Phe-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
Substrates: -
Products: -
Products: -
ir
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEA + Leu + Tyr + LVCGERGF + Phe + YTPKA
-
Substrates: oxidized insulin B chain, cleavage site specificity determination
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
proteins + H2O
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
-
Substrates: gelatin
Products: -
Products: -
ir
proteins + H2O
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
-
Substrates: more restricted specificity than pepsin A
Products: -
Products: -
ir
proteins + H2O
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
-
Substrates: little activity with hemoglobin
Products: -
Products: -
ir
additional information
?
-
-
Substrates: milk clotting activity examined
Products: -
Products: -
?
additional information
?
-
-
Substrates: little if any activity with hemoglobin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows generally low proteolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has milk-clotting activity. Its unspecific proteolytic activity hydrolyses bonds with Phe, Tyr, Leu or Val residues favouring the formation of undesirable peptides
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme shows milk clotting activity
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
Proteins + H2O
?
-
Substrates: enzyme formed from pepsinogen B, more restricted specificity than pepsin A
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SDS
-
When SDS concentration is below its critical micellar concentration (less than 0.05% (w/v)), the enzyme activity is reduced about 50% of its initial value. When SDS concentration is at 0.05% (w/v) or above, a 10% or less of its initial value is obtained
additional information
-
cetyltrimethyl ammonium bromide, Tween 80, and Triton X-100 do not alter the enzymatic activity at any concentration assayed
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation of pepsinogen B to pepsin B rapidly at pH 2, more slowly at pH 4, pepsinogen B contains 1 mol phosphate per mol enzyme, function unclear
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
56.14 U/mg protein. One unit is defined as the amount causing an increase of 1.0 in absorbance at 280 nm per min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5.5
-
hemoglobin, pH 1: about 50% of maximum activity, pH 5.5: about 10% of maximum activity
2.5 - 5
-
pH 2.5: about 20% of maximal activity, pH 3.0: about 70% of maximal activity, pH 4.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 57
-
haemoglobin, 2°C: about 55% of maximum activity, 57°C: about 30% of maximum activity, Q10 for milk clotting activity
20 - 55
-
20°C: about 35% of maximal activity, 50°C: about 60% of maximal activity, 55°C: about 25% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (156 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
pepssinogen B is proteolytically activated in the gastric tract, first cleavage site is Met16-Glu17, convertion at pH 5.5, not at pH 2.0
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F219S
mutant exhibits broad activity against various peptides, with retention of high activity against peptides with Gly at P2
Y13A
mutant shows new hydrolytic activity against several peptides, whereas the activity against peptides with Gly at P2 is decreased significantly. The newly obtained activity of the Tyr13Ala mutant is low
Y13A/F219S
mutant demonstrats general proteolytic activity, hydrolyzing various types of peptides very efficiently, although activity against peptides with Gly at P2 is decreased. The activity against typical peptides, such as KPAEFARL, KPAEFLRL, and KPGEFARL, is increased about 40times by the double mutation. The extent being much higher than that with single mutations
L287G
-
the mutation leads to a significant decrease in proteolytic activity. The mutant show an increase in the ratio of clotting activity to proteolytic activity compared to the wild type enzyme
T218A
-
the mutation leads to a significant decrease in proteolytic activity
T218S
additional information
-
low pH inactivation of viruses including porcine circovirus (PCV) type 1 (PCV1) and PCV1 removal by cation exchange chromatography (CEX) in the presence of pepsin, which is used for oral rotavirus vaccines production. Both parvovirus and PCV1 are contaminants in the vaccine production and can be effectively inactivated by low pH, and PCV1 can be removed by POROS 50HS CEX to finally receive a contaminant-free pepsin sample. Method development and evaluation, overview
T218S
-
the mutation causes a low thermostability and moderate increase in the clotting activity
T218S
-
the mutation leads to a significant decrease in proteolytic activity. The mutant show an 3.34fold increase in the ratio of clotting activity to proteolytic activity compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high pressure homogenization increases the milk-clotting activity of the enzyme processed at 150 MPa, being 15% higher than the milk-clotting activity of non-processed samples
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native pepsinogen by gel filtration and anion exchange chromatography to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
the enzyme's milk-clotting activity is used for cheese making. Mutant enzyme T218S serves as a milk coagulant that contributes to an optimal flavor development in mature cheese
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Unger, W.G.; Watkins, J.; Stamford, I.F.
Degradation of human serum albumin by human pepsins
Biochem. J.
113
8p-9p
1969
Sus scrofa
brenda
Gordon, S.; Werb, Z.
Secretion of macrophage neutral proteinase is enhanced by colchicine
Proc. Natl. Acad. Sci. USA
73
872-876
1976
Mus musculus
brenda
Arunchalam, K.; Haard, N.F.
Isolation and characterization of pepsin from polar cod (Boreogadus saida)
Comp. Biochem. Physiol. B
80B
467-473
1985
Boreogadus saida
-
brenda
Nielsen, P.K.; Foltmann, B.
Purification and characterization of porcine pepsinogen B and pepsin B
Arch. Biochem. Biophys.
322
417-422
1995
Sus scrofa
brenda
Foltmann, B.; Szecsi, P.B.
Pepsin B
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
28-29
2004
Sus scrofa
-
brenda
Klomklao, S.; Kishimura, H.; Yabe, M.; Benjakul, S.
Purification and characterization of two pepsins from the stomach of pectoral rattail (Coryphaenoides pectoralis)
Comp. Biochem. Physiol. B
147B
682-689
2007
Albatrossia pectoralis
brenda
Kageyama, T.
Roles of Tyr13 and Phe219 in the unique substrate specificity of pepsin B
Biochemistry
45
14415-14426
2006
Canis lupus familiaris (Q2AB25), Canis lupus familiaris
brenda
Leite Junior, B.R.; Tribst, A.A.; Cristianini, M.
High pressure homogenization of porcine pepsin protease effects on enzyme activity, stability, milk coagulation profile and gel development
PLoS ONE
10
e0125061
2015
Sus scrofa
brenda
Zhang, J.; Sun, Y.; Li, Z.; Luo, Q.; Li, T.; Wang, T.
Structure-based design of Mucor pusillus pepsin for the improved ratio of clotting activity/proteolytic activity in cheese manufacture
Protein Pept. Lett.
22
660-667
2015
Rhizomucor pusillus
-
brenda
Guzman, M.L.; Marques, M.R.; Olivera Me, M.E.; Stippler, E.S.
Enzymatic activity in the presence of surfactants commonly used in dissolution media, part 1 Pepsin
Results Pharma Sci.
6
15-19
2016
Sus scrofa
brenda
Yang, B.; Wang, H.; Kaleas, K.; Butler, M.; Franklin, J.; Bill, A.; Baylis, S.A.; Chen, Q.; Bluemel, J.
Clearance of porcine circovirus and porcine parvovirus from porcine-derived pepsin by low pH inactivation and cation exchange chromatography
Biotechnol. Prog.
36
e2968
2020
Sus scrofa
brenda
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