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Gene Review

hutU  -  urocanate hydratase

Pseudomonas putida KT2440

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Disease relevance of hutU


High impact information on hutU


Chemical compound and disease context of hutU


Biological context of hutU

  • The histidine utilization genes hutH and hutU of Pseudomonas putida ATCC 12633 have been mapped by interrupted mating and transduction to a location at approximately 43 minutes on the chromosome, closely linked to ser-800 and met-400 markers previously shown to be at 46 and 42 minutes, respectively [10].
  • The inactivation of urocanase was irreversible, could be partially blocked by the competitive inhibitor imidazolepropionate, and involved the modification of a single active-site thiol [8].

Associations of hutU with chemical compounds

  • When cloned individually with hutC on the same vector, hutF and hutU (which encodes urocanase) expression was induced by urocanate, indicating that these two genes each possess an operator-promoter element [11].
  • Urocanase from Ps. testosteroni does not contain pyridoxal 5'-phosphate as a coenzyme and in this respect is similar to all urocanases studied in purified form [7].
  • The inhibition resulted from oxidative decomposition of 4'(5')-imidazolone-5'(4')-propionate but was not due to the formation of the major degradative product, 4-ketoglutaramate, since this compound was not an irreversible inactivator of urocanase although it did produce some inhibition at high concentrations [8].
  • We conclude that in P. putida cysteine sulfinate or hypotaurine is catabolized in vivo by a transaminase reaction to sulfite, which modifies urocanase to a form that can be photoactivated [9].
  • Porcine crystalline transaminase caused reversion of highly purified P. putida urocanase with cysteine sulfinate and alpha-ketoglutarate [9].

Analytical, diagnostic and therapeutic context of hutU

  • 5. Form A of urocanase showed, after treatment with NaBH4 up to 50% inhibition, an elution pattern (TSK-DEAE column) similar to a mixture of forms A, B and C in the approximate ratio of 1:2:1 [12].
  • 1. Urocanase, purified by classical methods [Keul, V., Kaeppeli, F., Ghosh, C., Krebs, T., Robinson, J. A. and Rétey, J. (1979) J. Biol. Chem. 254, 843-851] from Pseudomonas putida was submitted to high-performance liquid chromatography on a TSK-DEAE column [12].


  1. Cloning and sequencing the urocanase gene (hutU) from Pseudomonas putida. Fessenmaier, M., Frank, R., Retey, J., Schubert, C. FEBS Lett. (1991) [Pubmed]
  2. Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida. Consevage, M.W., Porter, R.D., Phillips, A.T. J. Bacteriol. (1985) [Pubmed]
  3. Activation of urocanase from Pseudomonas putida by electronically excited triplet species. Venema, R.C., Hug, D.H. J. Biol. Chem. (1985) [Pubmed]
  4. Identification of the prosthetic group of urocanase. The mode of its reaction with sodium borohydride and of its photochemical reactivation. Keul, V., Kaeppeli, F., Ghosh, C., Krebs, T., Robinson, J.A., Rétey, J. J. Biol. Chem. (1979) [Pubmed]
  5. Cloning, expression and mutational analysis of the urocanase gene (hutU) from Pseudomonas putida. Lenz, M., Rétey, J. Eur. J. Biochem. (1993) [Pubmed]
  6. Photoactivation of urocanase in Pseudomonas putida. Role of sulfite in enzyme modification. Hug, D.H., O'Donnell, P.S., Hunter, J.K. J. Biol. Chem. (1978) [Pubmed]
  7. The purification and properties of urocanase from Pseudomonas testosteroni. Hacking, A.J., Bell, M.V., Hassall, H. Biochem. J. (1978) [Pubmed]
  8. Substrate-mediated inactivation of urocanase from Pseudomonas putida. Evidence for an essential sulfhydryl group. Matherly, L.H., Phillips, A.T. Biochemistry (1980) [Pubmed]
  9. Roles of cysteine sulfinate and transaminase on in vitro dark reversion of urocanase in Pseudomonas putida. Hug, D.H., Hunter, J.K. J. Bacteriol. (1982) [Pubmed]
  10. A revised map location for the histidine utilization genes in Pseudomonas putida. King, R.S., Sechrist, L.L., Phillips, A.T. J. Basic Microbiol. (1994) [Pubmed]
  11. Organization and multiple regulation of histidine utilization genes in Pseudomonas putida. Hu, L., Phillips, A.T. J. Bacteriol. (1988) [Pubmed]
  12. The stoichiometry of the tightly bound NAD+ in urocanase. Separation and characterization of fully active and inhibited forms of the enzyme. Klepp, J., Rétey, J. Eur. J. Biochem. (1989) [Pubmed]
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