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
-
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
- 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
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
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Metals Ions
Metals Ions on EC 3.4.21.83 - Oligopeptidase B
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Ca2+
-
stimulates amidase and proteolytic activities, maximal activation of 25% at concentrations above 25 mM
Ca2+
-
in presence of Ca2+, efficiency of hydrolysis of substrates with positively charged P2 residues decreases by an order of magnitude due to the worsening in the substrate binding. In the presence of 50 mM Ca2+, no substrate inhibition is observed in the case of acetyl-L-Leu-L-Lys-L-Arg-4-nitroanilide, and the effect was less pronounced for other substrates
Ca2+
calcium ions impede the reverse transition to the closed form. The reduction in the thermal stability of PSP in the presence of Ca2+ can be attributed to the destruction of the salt bridges SB2 and SB3 that takes place as Ca2+ binds to the E494 and D460 residues parxadtaking in bridge formation. Calcixadum ions are a destabilizing factor for all PSP mutant variants, overview