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Information on EC 3.4.21.83 - Oligopeptidase B and Organism(s) Escherichia coli and UniProt Accession P24555
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3.4.21.83 Oligopeptidase BSpecify your search results
Word Map
- 3.4.21.83
- gingivalis
-
prolyl
- leupeptin
-
chymotrypsin-like
- antipain
- porphyromonas
- aprotinin
-
chloromethyl
- chymostatin
- tlck
- tryptase
-
2-macroglobulin
- benzamidine
- acrosin
-
phenylmethanesulfonyl
- proteamaculans
-
bapna
- drug development
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trypsin-like protease, oligopeptidase b, protease ii, op-tb, la_opb, opbtc, tb-op, tc-op, tc 120, oligopeptidase b2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Protease II
-
-
-
-
Proteinase, Escherichia coli alkaline, II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
57657-67-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoyl-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
RRRPRPPRLPRPRPR + 2 H2O
L-Arg-L-Arg + RPRPPR + LPRPRPR
proline-rich peptide Bac(1-16)
-
-
?
RRRPRPPYLPRPRPPPFF + H2O
L-Arg-L-Arg + RPRPPYLPRPRPPPFF
proline-rich peptide PR-39(1-18)
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Arg-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Glu-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Benzoyl-Lys 2-naphthylamide + H2O
Benzoyl-Lys + 2-naphthylamine
-
-
-
-
?
N-Benzoyl-DL-Arg 4-nitroanilide + H2O
N-Benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
N-Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
N-Benzyloxycarbonyl-Gly + 4-nitrophenol
-
weak
-
-
?
N-benzyloxycarbonyl-Lys benzyl ester + H2O
N-benzyloxycarbonyl-Lys + benzyl alcohol
-
-
-
-
?
N-carbobenzoxy-L-Lys 4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
-
-
-
-
?
Nalpha-benzoyl-Arg-7-amido-4-methylcoumarin + H2O
?
-
68% of the activity with carbobenzoxy-Arg-Arg-4-methylcoumaryl-7-amide
-
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-7-amido-4-methylcoumarin + H2O
?
-
specific substrate for Escherichia coli oligopeptidase B, 20% of the activity with carbobenzoxy-Arg-Arg-4-methylcoumaryl-7-amide
-
-
?
Insulin B-chain + H2O
?
-
cleaves the carboxymethylated B-chain of insulin at the Arg22-Gly23 bond, but after prolonged periods of incubation it is also able to cleave the Tyr16-Leu17 bond
-
-
?
Insulin B-chain + H2O
?
-
cleavage at the carboxyl sides of Arg and Lys residues
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
?
additional information
?
-
OpdB does not hydrolyse protein substrates with the exception of nominal digestion of the endogenous Escherichia coli enzymes aspartokinase L-homoserine dehydrogenase and aspartokinase III
-
-
?
additional information
?
-
oligopeptidase B can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the P1 and P2 positions
-
-
?
additional information
?
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-
oligopeptidase B can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the P1 and P2 positions
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-
?
additional information
?
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hydrolyzes peptides with dibasic sites much faster than monobasic substrates, hydrolyzes the peptide bond at lysine and arginine residues
-
?
additional information
?
-
-
specific for substrates with a pair of basic residues at positions P1 and P2
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
stimulates amidase and proteolytic activities, maximal activation of 25% at concentrations above 25 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protamines
protamines, basic 30-32 residue peptides that are rich in Arg residues, are potent inhibitors of OpdB
-
benzoyl-Arg-4-nitroanilide
-
enzyme is inhibited by high concentrations of substrate
trans-4-guanidinomethylcyclohexanecarboxylic acid 4-tert-butylphenyl ester
-
IC50: about 0.01 mM. Oligopeptidase B is much more sensitive than oligopeptidase B
additional information
no inhibition by N-ethylmaleimide and iodoacetic acid. This is consistent with the absence of a cysteine residue at position 256 which is replaced by His
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
trans-4-guanidinomethylcyclohexanecarboxylic acid 4-tert-butylphenyl ester
Escherichia coli
-
IC50: about 0.01 mM. Oligopeptidase B is much more sensitive than oligopeptidase B
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
124
substrate t-butyloxycarbonyl-Gly-Arg-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
126
substrate t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
170
substrate t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
220
substrate t-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
243
substrate t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin, pH 8.0, 30°C
328
substrate benzoyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
370
substrate t-butyloxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
382
substrate t-butyloxycarbonyl-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
408
substrate t-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
570
substrate benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin, pH 8.0, 30°C
90
substrate t-butyloxycarbonyl-Glu-Lys-Lys-7-amido-4-methylcoumarin, pH 8.0, 30°C
additional information
additional information
the specific activity of OpdB in Escherichia coli increases under conditions where the carbon levels are limiting
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25
-
optimum temperature for the reactions of amide substrates slightly below
25
-
the abnormally low temperature optimum may be caused by the disruption of the hydrogen bond formed between the enzyme and the NH group of the scissile peptide bond
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression of peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and its level of activity directly correlates with the degree of resistance
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
81860
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
mutation of Tyr452 confirmed that this residue is involved in the catalytic mechanism by stabilising the intermediate consisting of an oxoanion. Furthermore, it is shown that this oxanion binding site prevents non-productive substrate binding
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 5 weeks, without or with 25 and 50 mM CaCl2, the remaining activities are 88%, 50% and 32% respectively
-
-80°C, enzyme form A loses its activity after 3 months of storage, enzyme form B remains stable for more than one year
-
-80°C, maximal stability in dilute solutions at protein concentrations no less than 0.3 mg/ml, pH 7.8
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion expression of oligopeptidase B with an N-terminal histidine tag using pET28a as the expression vector. Although most of the recombinant OpdB is produced as inclusion bodies, the solubility of the recombinant protease increases significantly when expression temperature shifts from 37°C to 30°C
-
location of the protease II gene on the physical map of the Escherichia coli chromosome
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanatani, A.; Masuda, T.; Shimoda, T.; Misoka, F.; Lin, X.S.; Yoshimoto, T.; Tsuru, D.
Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme
J. Biochem.
110
315-320
1991
Escherichia coli
Pacaud, M.; Richaud, C.
Protease II from Escherichia coli. Purification and characterization
J. Biol. Chem.
250
7771-7779
1975
Escherichia coli
Tsuru, D.; Yoshimoto, T.
Oligopeptidase B: protease II from Escherichia coli
Methods Enzymol.
244
201-215
1994
Escherichia coli
Pacaud, M.
Protease II from Escherichia coli. Substrate specificity and kinetic properties
Eur. J. Biochem.
82
439-451
1978
Escherichia coli
Pacaud, M.
Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase
Eur. J. Biochem.
64
199-204
1976
Escherichia coli
Kanatani, A.; Yoshimoto, T.; Nagai, H.; Ito, K.; Tsuru, D.
Location of the protease II gene (ptrB) on the physical map of the Escherichia coli chromosome
J. Bacteriol.
174
7881
1992
Escherichia coli
Polgar, L.
Oligopeptidase B: a new type of serine peptidase with a unique substrate-dependent temperature sensitivity
Biochemistry
38
15548-15555
1999
Escherichia coli
Juhasz, T.; Szeltner, Z.; Renner, V.; Polgar, L.
Role of the oxyanion binding site and subsites S1 and S2 in the catalysis of oligopeptidase B, a novel target for antimicrobial chemotherapy
Biochemistry
41
4096-4106
2002
Escherichia coli
Yan, J.B.; Wang, G.Q.; Du, P.; Zhu, D.X.; Wang, M.W.; Jiang, X.Y.
High-level expression and purification of Escherichia coli oligopeptidase B
Protein Expr. Purif.
47
645-650
2006
Escherichia coli
Coetzer, T.H.; Goldring, J.P.; Huson, L.E.
Oligopeptidase B: a processing peptidase involved in pathogenesis
Biochimie
90
336-344
2008
Escherichia coli (P24555), Moraxella lacunata (Q59536), Rhodococcus erythropolis, Salmonella enterica, Treponema denticola, Trypanosoma brucei (Q382P7), Trypanosoma cruzi (Q4CW30)
Mohamed Mustafa, M.S.; Nakajima, Y.; Oyama, H.; Iwata, N.; Ito, K.
Assessment of substrate inhibition of bacterial oligopeptidase B
Biol. Pharm. Bull.
35
2010-2016
2012
Escherichia coli (P24555), Escherichia coli, Rhodococcus erythropolis (C0ZRJ2), Rhodococcus erythropolis, Serratia marcescens (K0J8D4), Serratia marcescens, Stenotrophomonas maltophilia (K0J2A4), Stenotrophomonas maltophilia
Mattiuzzo, M.; De Gobba, C.; Runti, G.; Mardirossian, M.; Bandiera, A.; Gennaro, R.; Scocchi, M.
Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides
J. Microbiol. Biotechnol.
24
160-167
2014
Escherichia coli (P24555), Escherichia coli
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