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Literature summary for 3.4.24.89 extracted from

  • Pichlo, C.; Juetten, L.; Wojtalla, F.; Schacherl, M.; Diaz, D.; Baumann, U.
    Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1 (2019), J. Biol. Chem., 294, 11525-11535 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.89

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia BL21 Star (DE3) cells Clostridioides difficile

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Clostridioides difficile

Protein Variants

Protein Variants Comment Organism
E143A/Y178F inactive Clostridioides difficile
E184A the mutant shows reduced activity for Abz-DVVNPPVPPSKDD-CONH2 (15%) and Abz-DVVNAPVPPSKDD-CONH2 (9%) and residual activity for Abz-DVVNPAVPPSKDD-CONH2 (1.2%) compared to the wild type enzyme Clostridioides difficile
E184K the mutant shows residual activity compared to the wild type enzyme Clostridioides difficile
K101A the mutant shows dramatically reduced activity compared to the wild type enzyme Clostridioides difficile
K101E the mutant shows dramatically reduced activity compared to the wild type enzyme Clostridioides difficile
K101R the mutant shows about wild type activity Clostridioides difficile
W103A inactive Clostridioides difficile
W103F the mutant shows residual activity for Abz-DVVNPPVPPSKDD-CONH2 compared to the wild type enzyme Clostridioides difficile
W103H the mutant shows residual activity for Abz-DVVNPPVPPSKDD-CONH2 compared to the wild type enzyme Clostridioides difficile
W103Y the mutant shows severely reduced activity for Abz-DVVNPPVPPSKDD-CONH2 and residual activity for Abz-DVVNPAVPPSKDD-CONH2 and Abz-DVVNAPVPPSKDD-CONH2 compared to the wild type enzyme Clostridioides difficile

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0436
-
 Abz-DVVNAPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
0.0825
-
 Abz-DVVNPAVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
0.1366
-
 Abz-DVVNPPVPPSKDD-CONH2 mutant enzyme E184A, at pH 7.5 and 20°C Clostridioides difficile
0.137
-
 Abz-DVVNPPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Ac-EPNAAVP-CONH2 + H2O Clostridioides difficile heat shock protein 90-derived peptide Ac-EPNA + AVP-CONH2
-
 ?
Ac-EPNAAVP-CONH2 + H2O Clostridioides difficile 630 heat shock protein 90-derived peptide Ac-EPNA + AVP-CONH2
-
 ?
Ac-HLLPPPS-CONH2 + H2O Clostridioides difficile immunoglobulin A1-derived peptide Ac-HLLP + PPS-CONH2
-
 ?
Ac-HLLPPPS-CONH2 + H2O Clostridioides difficile 630 immunoglobulin A1-derived peptide Ac-HLLP + PPS-CONH2
-
 ?
Ac-SLRPAPP-CONH2 + H2O Clostridioides difficile fibrinogen beta-derived peptide Ac-SLRP + APP-CONH2
-
 ?
adhesion molecule CD2831 + H2O Clostridioides difficile
-
 ?
-
 ?
adhesion molecule CD2831 + H2O Clostridioides difficile 630
-
 ?
-
 ?
adhesion molecule CD3246 + H2O Clostridioides difficile
-
 ?
-
 ?
adhesion molecule CD3246 + H2O Clostridioides difficile 630
-
 ?
-
 ?
additional information Clostridioides difficile the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity ?
-
 ?
additional information Clostridioides difficile 630 the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q183R7
-
-
Clostridioides difficile 630 Q183R7
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal-affinity chromatography and gel filtration Clostridioides difficile

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-DVVNAPVPPSKDD-CONH2 + H2O
-
 Clostridioides difficile Abz-DVVNA + PVPPSKDD-CONH2
-
 ?
Abz-DVVNPAVPPSKDD-CONH2 + H2O
-
 Clostridioides difficile Abz-DVVNP + AVPPSKDD-CONH2
-
 ?
Abz-DVVNPPVPPSKDD-CONH2 + H2O
-
 Clostridioides difficile Abz-DVVNP + PVPPSKDD-CONH2
-
 ?
Ac-EPNAAVP-CONH2 + H2O heat shock protein 90-derived peptide Clostridioides difficile Ac-EPNA + AVP-CONH2
-
 ?
Ac-EPNAAVP-CONH2 + H2O heat shock protein 90-derived peptide Clostridioides difficile 630 Ac-EPNA + AVP-CONH2
-
 ?
Ac-HLLPPPS-CONH2 + H2O immunoglobulin A1-derived peptide Clostridioides difficile Ac-HLLP + PPS-CONH2
-
 ?
Ac-HLLPPPS-CONH2 + H2O immunoglobulin A1-derived peptide Clostridioides difficile 630 Ac-HLLP + PPS-CONH2
-
 ?
Ac-SLRPAPP-CONH2 + H2O fibrinogen beta-derived peptide Clostridioides difficile Ac-SLRP + APP-CONH2
-
 ?
adhesion molecule CD2831 + H2O
-
 Clostridioides difficile ?
-
 ?
adhesion molecule CD2831 + H2O
-
 Clostridioides difficile 630 ?
-
 ?
adhesion molecule CD3246 + H2O
-
 Clostridioides difficile ?
-
 ?
adhesion molecule CD3246 + H2O
-
 Clostridioides difficile 630 ?
-
 ?
additional information the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity Clostridioides difficile ?
-
 ?
additional information the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity Clostridioides difficile 630 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 24000, SDS-PAGE Clostridioides difficile

Synonyms

Synonyms Comment Organism
CD2830
-
 Clostridioides difficile
PPEP-1
-
 Clostridioides difficile
proline-proline endopeptidase-1
-
 Clostridioides difficile

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.87
-
 Abz-DVVNPAVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
1.17
-
 Abz-DVVNPPVPPSKDD-CONH2 mutant enzyme E184A, at pH 7.5 and 20°C Clostridioides difficile
1.26
-
 Abz-DVVNAPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
4.3
-
 Abz-DVVNPPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8.565
-
 Abz-DVVNPPVPPSKDD-CONH2 mutant enzyme E184A, at pH 7.5 and 20°C Clostridioides difficile
10.545
-
 Abz-DVVNPAVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
28.899
-
 Abz-DVVNAPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile
31.386
-
 Abz-DVVNPPVPPSKDD-CONH2 wild type enzyme, at pH 7.5 and 20°C Clostridioides difficile