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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General Information
General Information on EC 3.4.21.83 - Oligopeptidase B
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evolution
malfunction
physiological function
additional information
four isoforms of oligopeptidase B are differentially expressed in BALB/c and BALB/c nude mice, the enzyme is overexpressed in nude mice-derived parasites. The enzyme is a serine peptidase restricted to bacteria, plants and trypanosomatids that hydrolyses peptides of up to 30 amino acids after basic residues, especially arginine
evolution
oligopeptidase B (OpdB) is a trypsin-like serine peptidase belonging to the prolyl oligopeptidase family
evolution
oligopeptidase B is a trypsin-like peptidase belonging to the family of serine prolyl oligopeptidases with a two-domain structure of the enzyme including C-terminal peptidase catalytic domain and N-terminal seven-bladed beta-propeller domain
evolution
oligopeptidase B is a trypsin-like serine peptidase from the family of prolylx02oligopeptidases that is named after the archetypical member of this family, prolyl oligopeptidase (SC clan, S9 family, EC 3.4.21.26). This family is characterized by the presence of an N-terminal beta-propeller domain preventing the penetration into the active center of voluminous globular proteins and of catalytic domain located in the C-terminal part of the molecule
evolution
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oligopeptidase B (OpdB) is a trypsin-like serine peptidase belonging to the prolyl oligopeptidase family
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evolution
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oligopeptidase B is a trypsin-like serine peptidase from the family of prolylx02oligopeptidases that is named after the archetypical member of this family, prolyl oligopeptidase (SC clan, S9 family, EC 3.4.21.26). This family is characterized by the presence of an N-terminal beta-propeller domain preventing the penetration into the active center of voluminous globular proteins and of catalytic domain located in the C-terminal part of the molecule
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PSP enzyme treated by immobilized chymotrypsin (PSP-Chtr with about 66 kDa) 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. Treatment of enzyme PSP with immobilized trypsin 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
malfunction
substitution of the corresponding charged amino acid residues for the unxadcharged ones in OpdB from Trypanosoma brucei significantly rexadduces the thermal stability of these mutants
malfunction
the removal of negatively charged Asp647 and Asp649 leads therefore to better binding of lysine at P2 substrate position and decreased binding of arginine at the same position
malfunction
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substitution of the corresponding charged amino acid residues for the unxadcharged ones in OpdB from Trypanosoma brucei significantly rexadduces the thermal stability of these mutants
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malfunction
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PSP enzyme treated by immobilized chymotrypsin (PSP-Chtr with about 66 kDa) 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. Treatment of enzyme PSP with immobilized trypsin 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
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knock-out of OPB results in the disappearance of the serine protease activity of Leishmania extracts. OPB null parasites show an elevated content of enolase protein. This enolase is enzymatically inactive and associated with the parasite membrane. OPB deletion results in a striking alteration in macrophage responses to Leishmania. Whereas wild type parasites elicited little, if any, response from infected macrophages, OPB deletion parasites induce a massive up-regulation in gene transcription. These OPB deletion parasites display decreased virulence in the murine footpad indection model
physiological function
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oligopeptidase B null mutant parasites grow at a significantly faster rate in vitro, and are as virulent as wild type strains during infection in mice. Parasites are revealed in extra vascular regions showing that OPB is not involved in assisting Trypanosoma brucei parasites to cross microvascular endothelial cells. Null mutants show an increase in discrete cysteine peptidase activities when compared to wild type strains. A significant increase of prolyl oligopeptidase activity is observed in mutant, but no concomitant increase in prolyl oligopeptidase protein levels
physiological function
overexpression of peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and its level of activity directly correlates with the degree of resistance
physiological function
oligopeptidase B is a virulence factor of Leishmania amazonensis. The enzyme is a serine peptidase restricted to bacteria, plants and trypanosomatids that hydrolyses peptides of up to 30 amino acids after basic residues, especially arginine
comparative structure of the enzyme using the structures of both closed form of OpdB from Leishmania major (PDB ID 2XE4) and open form of OpdB from Trypanosoma brucei (PDB ID 4BP8) as templates, overview
additional information
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comparative structure of the enzyme using the structures of both closed form of OpdB from Leishmania major (PDB ID 2XE4) and open form of OpdB from Trypanosoma brucei (PDB ID 4BP8) as templates, overview
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
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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
three-dimensional structures of both OPB isozymes are built by comparative modelling and used to perform a virtual screening of the ZINC database, overview. The analysis of the molecular electrostatic potential map of isozymes OPB and OPB2 Leishmania amazonensis surfaces shows different charges distribution profiles
additional information
three-dimensional structures of both OPB isozymes are built by comparative modelling and used to perform a virtual screening of the ZINC database, overview. The analysis of the molecular electrostatic potential map of isozymes OPB and OPB2 Leishmania amazonensis surfaces shows different charges distribution profiles
additional information
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three-dimensional structures of both OPB isozymes are built by comparative modelling and used to perform a virtual screening of the ZINC database, overview. The analysis of the molecular electrostatic potential map of isozymes OPB and OPB2 Leishmania amazonensis surfaces shows different charges distribution profiles
additional information
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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
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