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3.4.21.83: Oligopeptidase B

This is an abbreviated version!
For detailed information about Oligopeptidase B, go to the full flat file.

Word Map on EC 3.4.21.83

Reaction

Hydrolysis of -Arg-/-, -Lys-/- bonds in oligopeptides, even when P1' residue is proline =

Synonyms

La_OpB, oligopeptidase B, oligopeptidase B-like, oligopeptidase B2, OP-Tb, OPB, OPB2, OPBTc, Opd B, OpdB, Protease II, Proteinase, Escherichia coli alkaline, II, PSP, Spro_3467, Tb-OP, Tc 120, Tc-OP, trypsin-like protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.83 Oligopeptidase B

Inhibitors

Inhibitors on EC 3.4.21.83 - Oligopeptidase B

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-amino-N-[4-(dimethylaminomethyl)phenyl]propanamide
ZINC 37042497, shows the lowest estimated binding energy by AutoDock program. The selected docking pose is also located close to the catalytic site and interacts through hydrogen bonds with Glu539, Ser614, Arg704, Glu659, and Phe641 residues. As the compound is protonated, it also makes ionic interactions with Glu539 and Glu659. Besides, it also performs hydrophobic contacts with Tyr537, Phe641, Leu655, and Ala615; ZINC 37042497, the compound shows hydrogen bonds with Arg655 and Glu612 residues, and it also forms an ionic interaction with Glu612 and hydrophobic contacts with Leu608, Tyr490, Ala569, and Val656
(3R)-3-amino-N-[3-(1H-tetrazol-5-yl)phenyl]butanamide
ZINC 37608688, located close to the catalytic site. It interacts through hydrogen bonds with Glu612, Pro607, Arg655 and Tyr490, and hydrophobic interactions with His688 and Arg655; ZINC 37608688, the compound forms hydrogen bonds with Tyr537, Pro654, Glu659 and Arg704. Moreover, compound 3 participates on hydrophobic interactions with Ala615, Phe641, Leu653, and Val705
1-(5-hydroxy-pyridine-3-carbonyl)-pyrrolidine-2-carboxylic acid
ZINC 19735155; ZINC 19735155, interacts with the binding site through hydrogen bonds with Ser568 and Glu612, Pi-stacking with Tyr490, and salt bridges with Glu612 and Arg567
3,4-dichloroisocoumarin
4-(2-aminoethyl)benzenesulfonyl fluoride
4-(2-aminoethyl)benzenesulfonylfluoride
non-peptide irreversible serine-peptidase inhibitor
4-methylumbelliferyl-p-guanidobenzoate
active site titrant
acetyl-L-Leu-L-Lys-L-Arg-4-nitroanilide
-
-
acetyl-Thr-Arg-Arg
-
-
agmatine
reversible
antipain
antipain dihydrochloride
-
1 mM, 79% remaining activity
Aromatic amidines
-
-
-
benzamidine
benzoyl-Arg-4-nitroanilide
-
enzyme is inhibited by high concentrations of substrate
benzoyl-L-Pro-L-Phe-L-Arg-4-nitroanilide
-
-
bovine basic pancreatic trypsin inhibitor
substrate Nalpha-benzoyl-DL-Arg-4-nitroanilide, competitive
-
Ca2+
0.01 mM, 69% residual activity
chymostatin
-
0,1 mM, 45% inhibition
diisopropylfluorophosphate
non-peptide irreversible serine-peptidase inhibitor
EDTA
-
1.3 mM, 98% remaining activity, 20 mM, 57% remaining activity
iodoacetamide
-
-
iodoacetic acid
-
L-arginine
-
-
leupeptin
m-phenanthroline
substrates Nalpha-benzoyl-DL-Arg-4-nitroanilide, acetyl-Leu-Leu-Arg-4-nitroanilide, anticompetitive
methanol
incubation in 20% (v/v) methanol (10-20 h, 4°C) results in partial decomposition of the high molecular weight PSP-GroEL complex with precipitation of denatured chaperonin and a small (no more than 10%) loss of PSP activity
Mg2+
0.01 mM, 73% residual activity
Mn2+
0.01 mM, 73% residual activity
N-ethyl-2-oxo-benzimidazole-5-sulphonamide
ZINC 63887176; ZINC 63887176, interacting through hydrogen bond with Glu659 and Pi-Pi stacking interaction with Tyr537
N-ethylmaleimide
NaCl
-
loss of almost 50 and 70% of its activity in the presence of 0.2 and 1.0 M NaCl, respectively. Presence of NaCl does not disrupt the dimeric structure
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide
-
-
NEM
-
Cys256 is the reactive cysteine residue that mediates OpdB inhibition. Cys256 adducts occlude the P1 substrate-binding site, preventing substrate binding
o-phenanthroline
substrates Nalpha-benzoyl-DL-Arg-4-nitroanilide, acetyl-Leu-Leu-Arg-4-nitroanilide, anticompetitive
p-aminobenzamidine
p-chloromercuribenzoate
non-peptide irreversible serine-peptidase inhibitor
Pefabloc SC
Pentamidine
reversible competitive inhibitor
pepstatin
-
1 microM, 94% remaining activity
peptidyl chloromethyl ketone
irreversible peptidyl inhibitors
peptidyl diazomethyl ketone
irreversible peptidyl inhibitors
peptidyl phosphonate alpha-aminoalkyl diphenyl ester
irreversible peptidyl inhibitors
Phe-Pro-Arg-chloromethylketone
0.01 mM, no residual activity
phenylmethane sulfonyl fluoride
irreversible inhibition
phenylmethanesulfonyl fluoride
irreversible
phosphoramidon
-
0.57 mM, 96% remaining activity
protamine
reversible competitive inhibitor
protamines
protamines, basic 30-32 residue peptides that are rich in Arg residues, are potent inhibitors of OpdB
-
suramin
partial non-competitive inhibitor
tert-butoxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
in the case of added dithiothreitol, reduced glutathione, or oxidized glutathione, a high concentration of the substrate tert-butoxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin inhibits the enzyme activity. By contrast, addition of 1 M NaCl to either dithiothreitol, reduced glutathione, or oxidized glutathione or 1 M NaCl alone prevents substrate inhibition
Tos-LysCH2Cl
non-peptide irreversible serine-peptidase inhibitor
tosyl-L-Lys-chloromethylketone
0.1 mM, no residual activity
tosyl-Leu chloromethyl ketone
-
-
trans-4-guanidinomethylcyclohexanecarboxylic acid 4-tert-butylphenyl ester
-
IC50: about 0.01 mM. Oligopeptidase B is much more sensitive than oligopeptidase B
ZnCl2
substrate Nalpha-benzoyl-DL-Arg-4-nitroanilide, noncompetitive
additional information
-