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Literature summary for 3.4.21.83 extracted from

  • Coetzer, T.H.; Goldring, J.P.; Huson, L.E.
    Oligopeptidase B: a processing peptidase involved in pathogenesis (2008), Biochimie, 90, 336-344.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cysteine
-
Trypanosoma brucei
dithiothreitol
-
Trypanosoma brucei
glutathione
-
Trypanosoma brucei

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure solved at 2.7 A resolution Trypanosoma brucei

Protein Variants

Protein Variants Comment Organism
C559S mutant shows significant decrease in activation by reducing agents. This residue may thus mediate the activity enhancing effect of reducing agents Trypanosoma brucei
C597S mutant shows significant decrease in activation by reducing agents. This residue may thus mediate the activity enhancing effect of reducing agents Trypanosoma brucei
additional information cys256 is identified as the reactive cysteine residue responsible for inactivation by N-ethylmaleimide and iodoacetic acid Trypanosoma brucei
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 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin non-peptide irreversible serine-peptidase inhibitor Trypanosoma brucei
4-(2-aminoethyl)benzenesulfonylfluoride non-peptide irreversible serine-peptidase inhibitor Trypanosoma brucei
4-methylumbelliferyl-p-guanidobenzoate active site titrant Trypanosoma brucei
antipain reversible competitive inhibitor Trypanosoma brucei
diisopropylfluorophosphate non-peptide irreversible serine-peptidase inhibitor Trypanosoma brucei
iodoacetic acid
-
Trypanosoma brucei
leupeptin reversible competitive inhibitor Trypanosoma brucei
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 Escherichia coli
N-ethylmaleimide
-
Trypanosoma brucei
p-chloromercuribenzoate non-peptide irreversible serine-peptidase inhibitor Trypanosoma brucei
Pentamidine reversible competitive inhibitor Trypanosoma brucei
peptidyl chloromethyl ketone irreversible peptidyl inhibitors Trypanosoma brucei
peptidyl diazomethyl ketone irreversible peptidyl inhibitors Trypanosoma brucei
peptidyl phosphonate alpha-aminoalkyl diphenyl ester irreversible peptidyl inhibitors Trypanosoma brucei
protamine reversible competitive inhibitor Trypanosoma brucei
protamines protamines, basic 30-32 residue peptides that are rich in Arg residues, are potent inhibitors of OpdB Escherichia coli
suramin partial non-competitive inhibitor Trypanosoma brucei
Tos-LysCH2Cl non-peptide irreversible serine-peptidase inhibitor Trypanosoma brucei

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Escherichia coli 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
-
Trypanosoma cruzi

Organism

Organism UniProt Comment Textmining
Escherichia coli P24555
-
-
Moraxella lacunata Q59536
-
-
Rhodococcus erythropolis
-
-
-
Salmonella enterica
-
-
-
Treponema denticola
-
-
-
Trypanosoma brucei Q382P7
-
-
Trypanosoma cruzi Q4CW30
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the specific activity of OpdB in Escherichia coli increases under conditions where the carbon levels are limiting Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cleaves oxidised insulin B chain Escherichia coli ?
-
?
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 Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
oligopeptidase B
-
Rhodococcus erythropolis
oligopeptidase B
-
Salmonella enterica
oligopeptidase B
-
Treponema denticola
oligopeptidase B
-
Moraxella lacunata
oligopeptidase B
-
Trypanosoma brucei
oligopeptidase B
-
Trypanosoma cruzi
oligopeptidase B
-
Escherichia coli
OP-Tb
-
Trypanosoma brucei
Opd B
-
Rhodococcus erythropolis
Opd B
-
Salmonella enterica
Opd B
-
Treponema denticola
Opd B
-
Moraxella lacunata
Opd B
-
Trypanosoma cruzi
Opd B
-
Escherichia coli
Protease II
-
Rhodococcus erythropolis
Protease II
-
Salmonella enterica
Protease II
-
Treponema denticola
Protease II
-
Moraxella lacunata
Protease II
-
Escherichia coli
Tc 120
-
Trypanosoma cruzi

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00000181
-
antipain
-
Trypanosoma brucei
0.00001
-
protamine
-
Trypanosoma brucei
0.00003
-
leupeptin
-
Trypanosoma brucei
0.0034
-
Pentamidine
-
Trypanosoma brucei
0.0067
-
suramin
-
Trypanosoma brucei