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Literature summary for 3.4.21.83 extracted from

  • de Matos Guedes, H.L.; Carneiro, M.P.; Gomes, D.C.; Rossi-Bergmanmn, B.; Giovanni de Simone, S.
    Oligopeptidase B from L. amazonensis: molecular cloning, gene expression analysis and molecular model (2007), Parasitol. Res., 101, 853-863.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Oligopeptidase B is overexpressed in Escherichia coli as an N-terminally hexahistidine-tagged fusion protein Leishmania amazonensis

Crystallization (Commentary)

Crystallization (Comment) Organism
using the hanging-drop vapour-diffusion technique in 7%(w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation Leishmania amazonensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83490
-
predicted from cDNA Leishmania amazonensis

Organism

Organism UniProt Comment Textmining
Leishmania amazonensis A7XAB0
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-

Purification (Commentary)

Purification (Comment) Organism
purified by using using metal-affinity chromatography Leishmania amazonensis

Source Tissue

Source Tissue Comment Organism Textmining
additional information oligopeptidase B gene is expressed in all cycle stages Leishmania amazonensis
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Synonyms

Synonyms Comment Organism
La_OpB
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Leishmania amazonensis
oligopeptidase B
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Leishmania amazonensis