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Literature summary for 4.2.1.49 extracted from

  • Boreiko, S.; Silva, M.; Iulek, J.
    Crystallization and X ray diffraction data analyses of the enzyme urocanate hydratase from Trypanosoma cruzi (2016), Rev. Virt. Quim., 8, 678-686 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
the recombinant C-terminally His6-tagged protein is expressed in Escherichia coli Trypanosoma cruzi

Crystallization (Commentary)

Crystallization (Comment) Organism
the enzyme is crystallized in several conditions, with the best crystals obtained with 0.04 M dipotassium hydrogen phosphate, 16.00 % (w/v) polyethylene glycol 8000 and 22.0% (v/v) glycerol. X ray diffraction data are collected to 2.61 A resolution. The crystals belong to the monoclinic space group P21, with unit cell parameters a = 85.12, b = 137.63, c = 117.69 A, beta = 94.69° and are suitable for molecular replacement phasing Trypanosoma cruzi

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi Q4D9S6
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Trypanosoma cruzi CL Brener Q4D9S6
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Purification (Commentary)

Purification (Comment) Organism
-
Trypanosoma cruzi

General Information

General Information Comment Organism
metabolism the enzyme is involved in histidine degradation and is essential for the catabolic conversion of urocanate to 4-imidazolone-5-propionate, which finally yields glutamate and further glutamine and tricarboxylic acid cycle intemediates such as 2-oxo-pentanedioate Trypanosoma cruzi