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
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3.4.21.83
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gingivalis
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prolyl
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leupeptin
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chymotrypsin-like
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antipain
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porphyromonas
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aprotinin
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chloromethyl
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chymostatin
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tlck
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tryptase
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2-macroglobulin
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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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Cloned
Cloned on EC 3.4.21.83 - Oligopeptidase B
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expressed in Escherichia coli
expression in Escherichia coli
fusion expression of oligopeptidase B with an N-terminal histidine tag using pET28a as the expression vector. Although most of the recombinant OpdB is produced as inclusion bodies, the solubility of the recombinant protease increases significantly when expression temperature shifts from 37°C to 30°C
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location of the protease II gene on the physical map of the Escherichia coli chromosome
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Oligopeptidase B is overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein
opdB gene PCR amplified and expressed in Escherichia coli BL21(lambdaDE3)
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Oligopeptidase B is overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein
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Oligopeptidase B is overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein