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Literature summary for 3.4.24.18 extracted from

  • Schulze, A.; Wermann, M.; Demuth, H.U.; Yoshimoto, T.; Ramsbeck, D.; Schlenzig, D.; Schilling, S.
    Continuous assays for meprin alpha and beta using prolyl tripeptidyl aminopeptidase (PtP) from Porphyromonas gingivalis (2018), Anal. Biochem., 559, 11-16 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene MEP1A, recombinant expression of N-terminally Strep-tagged meprin alpha in Drosophila melanogaster S2 cells, which are stably transfected with pMT/BiP/V5-C-hMep alpha22-600 Homo sapiens
gene MEP1B, recombinant expression of meprin alpha in Pichia pastoris strain X-33 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
actinonin
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Homo sapiens
additional information
-
additional information enzyme kinetic data for meprin alpha suggests hyperbolic v/S characteristics Homo sapiens
0.024
-
KKGYVADAP-4-nitroanilide pH 7.5, 30°C, recombinant enzyme Homo sapiens
0.024
-
KKGYVADAP-4-nitroanilide pH 7.4, 30°C, recombinant enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Homo sapiens
Zn2+ required, a zinc-metalloprotease Homo sapiens
Zn2+ zinc-dependent metalloendoprotease Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16819
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the recombinant His6-tagged enzyme is activated by cleavage through trypsin Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally Strep-tagged meprin alpha22-600 from Drosophila melanogaster S2 cells by hydrophobic interaction chromatography in an expanded bed system, followed by Strep-tactin affinity chromatography, activation of the enzyme by trypsin, and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
KKGYVADAP-4-nitroanilide + H2O
-
Homo sapiens KKGYVA + DAP-4-nitroanilide
-
?
additional information meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position Homo sapiens ?
-
?
additional information the cleavage of a meprin alpha substrate leads to generation of the prolyl tripeptidyl aminopeptidase (PtP, EC 3.4.14.12) substrate, and the activity of PtP results in release of a chromophore or fluorophore, coupled assay method evaluation, overview Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
MEP1A
-
Homo sapiens
meprin A subunit alpha UniProt Homo sapiens
meprin alpha
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
KKGYVADAP-4-nitroanilide pH 7.5, 30°C, recombinant enzyme Homo sapiens
1
-
KKGYVADAP-4-nitroanilide pH 7.4, 30°C, recombinant enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens
7.5
-
-
Homo sapiens

General Information

General Information Comment Organism
evolution the astacin proteases meprin alpha and meprin beta are zinc-dependent metalloproteases of the metzincin superfamily Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
41.7
-
KKGYVADAP-4-nitroanilide pH 7.5, 30°C, recombinant enzyme Homo sapiens
41.7
-
KKGYVADAP-4-nitroanilide pH 7.4, 30°C, recombinant enzyme Homo sapiens