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Literature summary for 3.4.24.89 extracted from

  • Hensbergen, P.; Klychnikov, O.; Bakker, D.; Van Winden, V.; Ras, N.; Kemp, A.; Cordfunke, R.; Dragan, I.; Deelder, A.; Kuijper, E.; Corver, J.; Drijfhout, J.; Van Leeuwen, H.
    A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface Proteins (2014), Mol. Cell. Proteomics, 13, 1231-1244.
No PubMed abstract available
Search for more literature for 3.4.24.89

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Clostridioides difficile

Inhibitors

Inhibitors Comment Organism Structure
o-phenanthroline
-
 Clostridioides difficile

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.077
-
 Dabcyl-Lys-EVNPPPPD-EdansGlu pH 7.4, 3°C Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ presence of bound Zn2+ in the protein Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adhesion molecule CD2831 + H2O Clostridioides difficile
-
 ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites ?
adhesion molecule CD3246 + H2O Clostridioides difficile
-
 ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q183R7
-
-

Reaction

Reaction Comment Organism Reaction ID
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues preference for cleaving Pro-Pro bonds Clostridioides difficile
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adhesion molecule CD2831 + H2O
-
 Clostridioides difficile ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites ?
adhesion molecule CD3246 + H2O
-
 Clostridioides difficile ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules ?
Dabcyl-Lys-EVNPPPPD-EdansGlu + H2O
-
 Clostridioides difficile Dabcyl-Lys-EVNP + PPPD-EdansGlu
-
 ?
heat shock protein HSP90beta + H2O
-
 Clostridioides difficile ? cleavage between resiudue A702 and A703 ?
IgA2 heavy chain + H2O
-
 Clostridioides difficile ? cleavage within the hinge region PVP-PPPPC ?
KAAEEPNAAVPDEIK + H2O peptide based on the cleacage site of HSP90beta Clostridioides difficile KAAEEPNA + AVPDEIK
-
 ?
LPXTG cell surface protein CD2831 + H2O
-
 Clostridioides difficile ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites ?
LPXTG cell surface protein CD3246 + H2O
-
 Clostridioides difficile ? native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules ?
additional information enzyme has a preference for cleaving Pro-Pro bonds. No substrates: different collagen types, casein and gelatin, heat shock protein 90alpha Clostridioides difficile ?
-
 ?

Synonyms

Synonyms Comment Organism
CD2830
-
 Clostridioides difficile

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
19
-
 Dabcyl-Lys-EVNPPPPD-EdansGlu pH 7.4, 3°C Clostridioides difficile

Expression

Organism Comment Expression
Clostridioides difficile in all Peptoclostridium difficile strains tested the cd2830 gene is present additional information