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
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acrosin
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phenylmethanesulfonyl
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proteamaculans
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bapna
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drug development
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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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Subunits
Subunits on EC 3.4.21.83 - Oligopeptidase B
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dimer
monomer
additional information
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x * 78000, wild-type enzyme PSP, SDS-PAGE, x * 66000, recombinant truncated enzyme from PSP-Chtr, SDS-PAGE, x * 75000, native enzyme truncated by trypsin treatment, i.e. PSP-Tr, SDS-PAGE
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x * 78000, wild-type enzyme PSP, SDS-PAGE, x * 66000, recombinant truncated enzyme from PSP-Chtr, SDS-PAGE, x * 75000, native enzyme truncated by trypsin treatment, i.e. PSP-Tr, SDS-PAGE
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oligopeptidase B is characterized by localization of the catalytic triad (Ser532, Asp617, and His652 in PSP) and also of the substrate binding sites S1 (Glu576 and Asp578) and S2 (Asp460) in the C-terminal catalytic domain, and by an unusual structure of the N-terminal domain: it is a seven-bladed beta-propeller. Such structure allows oligopeptides to penetrate to the catalytic triad localized in the cavity at the interface of two domains and not to admit voluminous molecules of globular proteins to the active center
additional information
-
oligopeptidase B is characterized by localization of the catalytic triad (Ser532, Asp617, and His652 in PSP) and also of the substrate binding sites S1 (Glu576 and Asp578) and S2 (Asp460) in the C-terminal catalytic domain, and by an unusual structure of the N-terminal domain: it is a seven-bladed beta-propeller. Such structure allows oligopeptides to penetrate to the catalytic triad localized in the cavity at the interface of two domains and not to admit voluminous molecules of globular proteins to the active center
additional information
the enzyme has a two-domain structure of the enzyme including C-terminal peptidase catalytic domain and N-terminal seven-bladed beta-propeller domain
additional information
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the enzyme has a two-domain structure of the enzyme including C-terminal peptidase catalytic domain and N-terminal seven-bladed beta-propeller domain
additional information
-
oligopeptidase B is characterized by localization of the catalytic triad (Ser532, Asp617, and His652 in PSP) and also of the substrate binding sites S1 (Glu576 and Asp578) and S2 (Asp460) in the C-terminal catalytic domain, and by an unusual structure of the N-terminal domain: it is a seven-bladed beta-propeller. Such structure allows oligopeptides to penetrate to the catalytic triad localized in the cavity at the interface of two domains and not to admit voluminous molecules of globular proteins to the active center
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