EC Number   |
General Information |
Reference |
|---|
   3.4.21.83 | evolution |
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 |
755071 |
| 3.4.21.83 | evolution |
oligopeptidase B (OpdB) is a trypsin-like serine peptidase belonging to the prolyl oligopeptidase family |
-, 752409 |
| 3.4.21.83 | 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 |
752858 |
| 3.4.21.83 | 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 |
-, 752738 |
| 3.4.21.83 | malfunction |
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 |
-, 752738 |
| 3.4.21.83 | 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 |
-, 752409 |
| 3.4.21.83 | 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 |
752858 |
| 3.4.21.83 | more |
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 |
752858 |
| 3.4.21.83 | more |
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 |
-, 752738 |
| 3.4.21.83 | more |
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 |
754988 |
