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Literature summary for 4.2.1.51 extracted from

  • Vivan, A.L.; Caceres, R.A.; Abrego, J.R.; Borges, J.C.; Ruggiero Neto, J.; Ramos, C.H.; de Azevedo, W.F.; Basso, L.A.; Santos, D.S.
    Structural studies of prephenate dehydratase from Mycobacterium tuberculosis H37Rv by SAXS, ultracentrifugation, and computational analysis (2008), Proteins, 72, 1352-1362.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3), pET-23a(+) expression vector Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
predicted by dynamic light scattering Mycobacterium tuberculosis
134500
-
predicted as a tetrameric globular particle Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIC3 encoded by pheA gene (Rv3838c); H37Rv
-
Mycobacterium tuberculosis H37Rv P9WIC3 encoded by pheA gene (Rv3838c); H37Rv
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration, recombinant protein Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
three-dimensional enzyme structure, oligomeric state determined, circular dichroism method and bioinformatics tools, hydrodynamic properties, analytical ultracentrifugation experiments, small angle X-ray scattering, enzyme stability shown by molecular dynamics simulations, predicted as a flat disk protein with an asymmetric shape Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
homotetramer determined by small angle X-ray scattering and analytical ultracentrifugation Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
MtbPDT
-
Mycobacterium tuberculosis