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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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.83 - Oligopeptidase B
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proteolytic modification
treatment of enzyme PSP with immobilized trypsin (immobilized on modified porous glass) leads to production of a stable truncated enzyme form (PSP-Tr with about 75 kDa) which lacks 22 C-terminal amino acid residues and completely loses enzymatic activity, presumably because of changes in the nearest environment of His652 of the catalytic triad. The truncated enzyme, i.e. PSP-Chtr, prepared via cleavage with immobilized chymotrypsin (immobilized on modified porous glass) lacks the N-terminal region of the molecule that envelops the catalytic domain of PSP and supposedly prevents hydrolysis of high molecular weight substrates. The lacking fragment corresponds to the N-terminal highest rank element of the informational structure of PSP
proteolytic modification
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treatment of enzyme PSP with immobilized trypsin (immobilized on modified porous glass) leads to production of a stable truncated enzyme form (PSP-Tr with about 75 kDa) which lacks 22 C-terminal amino acid residues and completely loses enzymatic activity, presumably because of changes in the nearest environment of His652 of the catalytic triad. The truncated enzyme, i.e. PSP-Chtr, prepared via cleavage with immobilized chymotrypsin (immobilized on modified porous glass) lacks the N-terminal region of the molecule that envelops the catalytic domain of PSP and supposedly prevents hydrolysis of high molecular weight substrates. The lacking fragment corresponds to the N-terminal highest rank element of the informational structure of PSP
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