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Literature summary for 3.4.21.83 extracted from

  • Mikhailova, A.G.; Nekrasov, A.N.; Zinchenko, A.A.; Rakitina, T.V.; Korzhenevsky, D.A.; Lipkin, A.V.; Razguljaeva, O.A.; Ovchinnikova, M.V.; Gorlenko, V.A.; Rumsh, L.D.
    Truncated variants of Serratia proteamaculans oligopeptidase B having different activities (2015), Biochemistry (Moscow), 80, 1331-1343 .
    View publication on PubMed
Search for more literature for 3.4.21.83

General Stability

General Stability Organism
glycerol has a stabilizing influence on PSP during longx02term incubation Serratia proteamaculans

Inhibitors

Inhibitors Comment Organism Structure
additional information 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 Serratia proteamaculans

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Serratia proteamaculans

Organism

Organism UniProt Comment Textmining
Serratia proteamaculans A8GHH5
-
-
Serratia proteamaculans 568 A8GHH5
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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 Serratia proteamaculans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information azocasein is a substrate only of truncated enzyme PSP-Chtr, no activity with full-length PSP Serratia proteamaculans ?
-
 ?
additional information azocasein is a substrate only of truncated enzyme PSP-Chtr, no activity with full-length PSP Serratia proteamaculans 568 ?
-
 ?
Nalpha-benzoyl-DL-argininyl-4-nitroanilide + H2O i.e. BAPNA, substrate of wild-type enzyme PSP, lower activity with truncated enzyme PSP-Chtr Serratia proteamaculans Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
 ?
Nalpha-benzoyl-DL-argininyl-4-nitroanilide + H2O i.e. BAPNA, substrate of wild-type enzyme PSP, lower activity with truncated enzyme PSP-Chtr Serratia proteamaculans 568 Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
? 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 Serratia proteamaculans
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 Serratia proteamaculans

Synonyms

Synonyms Comment Organism
OpdB
-
 Serratia proteamaculans
PSP
-
 Serratia proteamaculans
Spro_3467
-
 Serratia proteamaculans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Serratia proteamaculans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Serratia proteamaculans

General Information

General Information Comment Organism
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 Serratia proteamaculans
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 Serratia proteamaculans
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 Serratia proteamaculans