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Literature summary for 3.4.22.B5 extracted from

  • Sanderson, S.J.; Pollock, K.G.J.; Hilley, J.D.; et al.
    Expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana (2000), Biochem. J., 347, 383-388.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.B5

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of CPB2.8 as an inactive pro-form lacking the characteristic C-terminal extension, CPB2.8DELTACTE in Escherichia coli. Pro-region processing is initiated during protein refolding and proceeds through several intermediate stages. Maximum enzyme activity after removal of the entire pro-region. This is facilitated by acidification Leishmania mexicana

Inhibitors

Inhibitors Comment Organism Structure
antipain
-
 Leishmania mexicana
E-64
-
 Leishmania mexicana
leupeptin effective inhibitor of the recombinant mature CPB2.8DELTACTE Leishmania mexicana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.083
-
 N-benzoyl-Pro-Phe-Arg-p-nitroanilide pH 6.0, 37°C Leishmania mexicana

Localization

Localization Comment Organism GeneOntology No. Textmining
inclusion body recombinant enzyme from Escherichia coli Leishmania mexicana 16234
-
inclusion body recombinant enzyme expressed in Escherichia coli Leishmania mexicana 16234
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
 x * 26000, activated enzyme, SDS-PAGE Leishmania mexicana

Organism

Organism UniProt Comment Textmining
Leishmania mexicana
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification overexpression of CPB2.8 as an inactive pro-form lacking the characteristic C-terminal extension, CPB2.8DELTACTE in Escherichia coli. Pro-region processing is initiated during protein refolding and proceeds through several intermediate stages. Maximum enzyme activity after removal of the entire pro-region. The activated enzyme has a MW of 26000 Da, the inactive pro-form of the enzyme has a MW of 38000 Da as determined by SDS-PAGE Leishmania mexicana

Purification (Commentary)

Purification (Comment) Organism
-
 Leishmania mexicana

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.16
-
-
 Leishmania mexicana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
-
 Leishmania mexicana N-benzoyl-Pro-Phe-Arg + p-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
? x * 26000, activated enzyme, SDS-PAGE Leishmania mexicana
More the inactive pro-form of the enzyme has a MW of 38000 Da as determined by SDS-PAGE Leishmania mexicana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
17.8
-
 N-benzoyl-Pro-Phe-Arg-p-nitroanilide pH 6.0, 37°C Leishmania mexicana