Information on EC 3.4.24.70 - oligopeptidase A

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.4.24.70
-
RECOMMENDED NAME
GeneOntology No.
oligopeptidase A
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
show the reaction diagram
-
-
-
-
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
show the reaction diagram
the Tyr607 residue is involved in the recognition of the substrate with a key role in catalysis, it plays an important role in the enzyme-substrate interaction and in the hydrolytic activity
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
148266-37-9
-
394250-11-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain BL21 (DE3) pLysS
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
TN3080
-
-
Manually annotated by BRENDA team
Escherichia coli BL21 (DE3) pLysS
strain BL21 (DE3) pLysS
-
-
Manually annotated by BRENDA team
Escherichia coli DH5
DH5
-
-
Manually annotated by BRENDA team
Escherichia coli TN3080
TN3080
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
-
-
-
Manually annotated by BRENDA team
PCC 7120
-
-
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-GASPFRQ-EDDnp + H2O
Abz-GA + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GDSPFRQ-EDDnp + H2O
Abz-GD + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GESPFRQ-EDDnp + H2O
Abz-GE + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GF + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GGSPFRQ-EDDnp + H2O
Abz-GG + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GHSPFRQ-EDDnp + H2O
Abz-GH + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GKSPFRQ-EDDnp + H2O
Abz-GK + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GLSPFRQ-EDDnp + H2O
Abz-GL + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GNSPFRQ-EDDnp + H2O
Abz-GN + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GPSPFRQ-EDDnp + H2O
Abz-GP + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GQSPFRQ-EDDnp + H2O
Abz-GQ + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GRSPFRQ-EDDnp + H2O
Abz-GR + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GSSPFRQ-EDDnp + H2O
Abz-GS + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GYSPFRQ-EDDnp + H2O
Abz-GY + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
show the reaction diagram
-
-
-
-
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
show the reaction diagram
-
-
-
-
-
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
show the reaction diagram
-
-
-
-
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
show the reaction diagram
Escherichia coli, Escherichia coli DH5
-
-
-
-
-
alpha-casein-derived peptides + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
-
-
-
-
-
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
show the reaction diagram
-
-
-
-
neurotensin + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli BL21 (DE3) pLysS
-
-
-
-
?
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
Escherichia coli, Escherichia coli BL21 (DE3) pLysS
-
-
-
-
?
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
Escherichia coli, Escherichia coli BL21 (DE3) pLysS
-
-
-
-
?
o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
best substrate for OpdA
-
-
?
o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
-
-
-
?
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
show the reaction diagram
-
-
smallest fragment: tripeptide
-
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
show the reaction diagram
-
proposed cleavage sites, methionine-labelled
peptide fragments identified
-
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
-
further degrades partially degraded portions of signal peptide yielded by protease IV
-
-
-
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
-
Bradykinin + H2O
?
show the reaction diagram
Escherichia coli, Escherichia coli BL21 (DE3) pLysS
-
-
-
-
?
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
?
-
-
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
-
-
?
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, 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
?
-
-
substrate specificities and cleavage sites of OpdA mutants, overview
-
-
-
additional information
?
-
Escherichia coli BL21 (DE3) pLysS
-
no cleavage of Abz-GFPPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
?
additional information
?
-
Escherichia coli TN3080
-
benzyloxycarbonyl-Gly-Gly-Gly-Gly or benzyloxycarbonyl-Gly-Gly-Gly-Gly-Gly
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
-
-
-
-
-
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
-
further degrades partially degraded portions of signal peptide yielded by protease IV
-
-
-
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
-
in vitro studies suggest oligopeptidase A may be involved in degradation of signal peptides
-
-
-
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
-
directly or indirectly involved in post-translational processing, required for normal growth of phage P22
-
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATP-dependent protease
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mn2+
-
activation, to a lesser extent than Co2+, 0.1 mM
Zn2+
-
dependent on
additional information
-
putative Zn2+-binding site
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
totally inhibits at 4 mM
Pro-Ile
-
partly inhibits
JA-2
-
totally inhibits at 0.003 mM
additional information
-
not inhibited by 0.2 mM leupeptin, 0.1 mM PMSF, 0.1 mM E-64, 0.001 mM Z-pro-prolinal and 0.02 mM captopril
-
additional information
-
not inhibited by captopril
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0008
-
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0042
-
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
-
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
-
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0011
-
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0004
-
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0004
-
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
-
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
-
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
-
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0022
-
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0002
-
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0005
-
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
-
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.5
-
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.2
-
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.08
-
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.1
-
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.2
-
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.74
-
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.4
-
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.5
-
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.5
-
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.1
-
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.6
-
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
2.4
-
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.3
-
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.5
-
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
595
-
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302688
49
-
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302696
42
-
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302695
1584
-
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302677
194
-
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302689
1920
-
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302697
1095
-
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302699
844
-
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302690
273
-
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302694
159
-
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302700
258
-
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302693
10360
-
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302698
590
-
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302692
2191
-
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
302691
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0662
-
-
with o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0833
-
-
with o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0858
-
-
with o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.1129
-
-
with o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.289
-
-
with o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
7.8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8
-
activity range, profile, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
37
-
-
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Escherichia coli TN3080
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
77100
-
-
gel filtration
additional information
-
-
amino acid sequence deduced from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
in OpdA, the flexible loop is formed by residues 600-614, 600SHIFAGGYAAGYYSY614, modeling studies, overview
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, in 0.25 M potassium phosphate buffer, pH 8, at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by nickel affinity chromatography
-
recombinant His-tagged wild-type OpdA and mutants from Escherichia coli strain DH5alpha by nickel affinity chromatography
-
to near homogeneity
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Escherichia coli, prlC-gene; nucleotide sequences; opdA-gene; Salmonella typhimurium
-
expressed from pHis3-OpdA
-
expression of His-tagged wild-type OpdA and mutants in Escherichia coli strain DH5alpha
-
gene opdA, DNA and amino acid sequence determination and anaylsis, expression of the His-tagged enzyme in strain BL21(DE3)
-
Escherichia coli, prlC-gene; nucleotide sequences; opdA-gene; Salmonella typhimurium
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Y607A
-
the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
Y607F
-
the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
additional information
-
supressors of the protein-localization defect conferred by certain signal sequence mutations