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GUEST COMMENTARY

Metabolic Versatility of Prokaryotes for Urea Decomposition

Robert P. Hausinger
Robert P. Hausinger
Department of Microbiology and Molecular Genetics and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824
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  • For correspondence: hausinge@msu.edu
DOI: 10.1128/JB.186.9.2520-2522.2004
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  • FIG. 1.
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    FIG. 1.

    Urease catalyzes the hydrolysis of urea, yielding one molecule each of ammonia and carbamate.

  • FIG. 2.
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    FIG. 2.

    Dinuclear nickel active site of urease. The structure depicted is that of urease from Klebsiella aerogenes (PDB accession code 1FWJ). A carbamylated lysine residue (indicated by K217*) bridges the two metal ions (shown in green), and metal-bound waters are illustrated in red.

  • FIG. 3.
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    FIG. 3.

    The three activities of urea amidolyase, biotin carboxylase, urea carboxylase, and allophanate hydrolase, are shown.

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Metabolic Versatility of Prokaryotes for Urea Decomposition
Robert P. Hausinger
Journal of Bacteriology Apr 2004, 186 (9) 2520-2522; DOI: 10.1128/JB.186.9.2520-2522.2004

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Metabolic Versatility of Prokaryotes for Urea Decomposition
Robert P. Hausinger
Journal of Bacteriology Apr 2004, 186 (9) 2520-2522; DOI: 10.1128/JB.186.9.2520-2522.2004
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    • UREASE
    • UREA AMIDOLYASE
    • REMAINING QUESTIONS
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KEYWORDS

Alphaproteobacteria
Urea

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