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Abz-GASPFRQ-EDDnp + H2O
Abz-GA + SPFRQ-EDDnp
-
-
-
-
?
Abz-GDSPFRQ-EDDnp + H2O
Abz-GD + SPFRQ-EDDnp
-
-
-
-
?
Abz-GESPFRQ-EDDnp + H2O
Abz-GE + SPFRQ-EDDnp
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GF + SPFRQ-EDDnp
-
-
-
-
?
Abz-GGSPFRQ-EDDnp + H2O
Abz-GG + SPFRQ-EDDnp
-
-
-
-
?
Abz-GHSPFRQ-EDDnp + H2O
Abz-GH + SPFRQ-EDDnp
-
-
-
-
?
Abz-GKSPFRQ-EDDnp + H2O
Abz-GK + SPFRQ-EDDnp
-
-
-
-
?
Abz-GLSPFRQ-EDDnp + H2O
Abz-GL + SPFRQ-EDDnp
-
-
-
-
?
Abz-GNSPFRQ-EDDnp + H2O
Abz-GN + SPFRQ-EDDnp
-
-
-
-
?
Abz-GPSPFRQ-EDDnp + H2O
Abz-GP + SPFRQ-EDDnp
-
-
-
-
?
Abz-GQSPFRQ-EDDnp + H2O
Abz-GQ + SPFRQ-EDDnp
-
-
-
-
?
Abz-GRSPFRQ-EDDnp + H2O
Abz-GR + SPFRQ-EDDnp
-
-
-
-
?
Abz-GSSPFRQ-EDDnp + H2O
Abz-GS + SPFRQ-EDDnp
-
-
-
-
?
Abz-GYSPFRQ-EDDnp + H2O
Abz-GY + SPFRQ-EDDnp
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
alpha-casein-derived peptides + H2O
?
-
alpha-casein is not cleaved by OpdA, but by proteases HslUV, ClpAP, or Lon, the peptide products are then cleaved by OpdA, overview
-
-
?
bacteriophage P22 gp7 protein
?
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
best substrate for OpdA
-
-
?
o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
Prolipoprotein signal peptide + H2O
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
additional information
?
-
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
-
directly or indirectly involved in post-translational processing, required for normal growth of phage P22
-
-
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
-
-
-
-
?
Prolipoprotein signal peptide + H2O
?
-
further degrades partially degraded portions of signal peptide yielded by protease IV
-
-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
?
Prolipoprotein signal peptide + H2O
?
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
-
smallest fragment: tripeptide
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
proposed cleavage sites
peptide fragments identified
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
methionine-labelled
peptide fragments identified
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
-
-
smallest fragment: tripeptide
?
additional information
?
-
-
benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
-
-
?
additional information
?
-
-
substrates are N-blocked peptides with at least 4 amino acid residues or unblocked pentapeptides, no substrates are signal peptide still attached to the mature protein
-
-
?
additional information
?
-
-
no cleavage of Abz-GFPPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
?
additional information
?
-
-
substrate specificities and cleavage sites of OpdA mutants, overview
-
-
?
additional information
?
-
-
no cleavage of Abz-GFPPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
?
additional information
?
-
-
the enzyme digests proteins to short peptides that are subsequently hydrolyzed to smaller fragments and free amino acids, protein degradation is an essential quality control and regulatory function
-
-
?
additional information
?
-
-
the enzyme cleaves peptides generated by the activity of the three primary ATP-dependent proteases Lon, HslUV, and ClpAP from Escherichia coli, overview
-
-
?
additional information
?
-
-
benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
-
-
?
additional information
?
-
-
benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
-
-
?
additional information
?
-
-
hydrolyzes N-blocked peptides containing at least four amino acids but is unable to hydrolyze unblocked peptides with fewer than five amino acids, Gly or Ala on either side of the scissile bond is permissive for hydrolysis
-
-
?
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0.0008
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0042
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0018
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0007
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0011
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0004
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0004
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0018
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0018
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0007
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0022
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0002
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0005
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.0007
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
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0.5
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.2
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.08
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1.1
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.2
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.74
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.4
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1.5
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.5
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.1
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.6
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
2.4
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.3
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1.5
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
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595
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
49
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
42
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1584
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
194
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1920
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
1095
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
844
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
273
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
159
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
258
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
10360
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
590
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
2191
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37°C, recombinant wild-type enzyme
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malfunction
plants with defective enzyme expression exhibit heightened resistance to exogenous salicylate treatment
metabolism
isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death. TOP1 and TOP2 expression are coordinately regulated during pathogen-associated molecular pattern-triggered plant immunity
evolution
the TOP isozymes contain the conserved His-Glu-XX-His (HEXXH) sequence of active-site residues and belong to the M3 family of metallopeptidases
evolution
the TOP isozymes contain the conserved His-Glu-XX-His (HEXXH) sequence of active-site residues and belong to the M3 family of metallopeptidases. TOP1 and TOP2 are located on opposite ends of chromosome 5 and share high homology, indicating the occurrence of a past intra-chromosomal duplication event
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, but through independent pathways
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, they are necessary for the immune response to avirulent pathogens. Isozyme TOP1 induces the augmentation of expression of isozyme TOP2 by the flagellin peptide flg22. Isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, they are necessary for the immune response to avirulent pathogens. Isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death
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Conlin, C.A.; Miller, C.G.
Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium
Methods Enzymol.
248
567-579
1995
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli TN3080
brenda
Novak, P.; Dev, I.K.
Degradation of a signal peptide by protease IV and oligopeptidase A
J. Bacteriol.
170
5067-5075
1988
Escherichia coli
brenda
Conlin, C.A.; Vimr, E.R.; Miller, C.G.
Oligopeptidase A is required for normal phage P22 development
J. Bacteriol.
174
5869-5880
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Conlin, C.A.; Trun, N.J.; Silhavy, T.J.; Miller, C.G.
Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene
J. Bacteriol.
174
5881-5887
1992
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli DH5
brenda
Conlin, C.A.; Miller, C.G.
Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium
J. Bacteriol.
174
1631-1640
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Novak, P.; Ray, P.H.; Dev, I.K.
Localization and purification of two enzymes from Escherichia coli capable of hydrolyzing a signal peptide
J. Biol. Chem.
261
420-427
1986
Escherichia coli
brenda
Paschoalin, T.; Carmona, A.K.; Oliveira, V.; Juliano, L.; Travassos, L.R.
Characterization of thimet- and neurolysin-like activities in Escherichia coli M3A peptidases and description of a specific substrate
Arch. Biochem. Biophys.
441
25-34
2005
Escherichia coli, Escherichia coli BL21 (DE3) pLysS
brenda
Miller, C.G.
Oligopeptidase A
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
362-363
2004
Azotobacter vinelandii, Aeromonas hydrophila, Synechocystis sp., Arabidopsis thaliana, Burkholderia pseudomallei, Deinococcus radiodurans, Escherichia coli, Salmonella enterica, Avibacterium paragallinarum, Haemophilus influenzae, Leptospira interrogans, Neisseria meningitidis, Nitrosomonas europaea, no activity in Methanocaldococcus jannaschii, Nostoc punctiforme, Nostoc sp., Pasteurella multocida, Yersinia pestis, Plasmodium yoelii, Prochlorococcus marinus, Proteus vulgaris, Pseudomonas aeruginosa, Pseudomonas fluorescens, Ralstonia solanacearum, Pseudomonas syringae, Cupriavidus metallidurans, Salmonella enterica subsp. enterica serovar Typhimurium, Shewanella oneidensis, Shigella flexneri, Synechococcus sp., Xanthomonas campestris, Xylella fastidiosa, Paraburkholderia fungorum, Xanthomonas axonopodis, Saccharophagus degradans, Thermosynechococcus vestitus, Trichodesmium erythraeum, Histophilus somni, Vibrio cholerae serotype O1, Synechococcus sp. WH 8102
-
brenda
Jain, R.; Chan, M.K.
Support for a potential role of E. coli oligopeptidase A in protein degradation
Biochem. Biophys. Res. Commun.
359
486-490
2007
Escherichia coli K-12
brenda
Lorenzon, R.Z.; Cunha, C.E.; Marcondes, M.F.; Machado, M.F.; Juliano, M.A.; Oliveira, V.; Travassos, L.R.; Paschoalin, T.; Carmona, A.K.
Kinetic characterization of the Escherichia coli oligopeptidase A (OpdA) and the role of the Tyr(607) residue
Arch. Biochem. Biophys.
500
131-136
2010
Escherichia coli
brenda
Wang, R.; Rajagopalan, K.; Sadre-Bazzaz, K.; Moreau, M.; Klessig, D.; Tong, L.
Structure of the Arabidopsis thaliana TOP2 oligopeptidase
Acta Crystallogr. Sect. F
70
555-559
2014
Arabidopsis thaliana (Q949P2), Arabidopsis thaliana (Q94AM1)
brenda
Moreau, M.; Westlake, T.; Zampogna, G.; Popescu, G.; Tian, M.; Noutsos, C.; Popescu, S.
The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response
Plant J.
76
603-614
2013
Arabidopsis thaliana (Q949P2), Arabidopsis thaliana (Q94AM1)
brenda
Anu, P.; Madanan, M.; Nair, A.; Nair, G.; Nair, G.; Sudhakaran, P.; Satheeshkumar, P.
Heterologous expression, purification and characterization of an oligopeptidase A from the pathogen Leptospira interrogans
Mol. Biotechnol.
60
302-309
2018
Leptospira interrogans serovar Copenhageni (Q72SL8), Leptospira interrogans serovar Copenhageni Fiocruz L1-130 (Q72SL8)
brenda