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Gene Review

gatA-3  -  amidase

Sulfolobus solfataricus P2

 
 
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Disease relevance of gatA-3

  • We have cloned, sequenced, and overexpressed in Escherichia coli the amidase gene from the hyperthermophilic archaeon Sulfolobus solfataricus (strain MT4) [1].
  • We report here that this enzyme also converts nitriles in the corresponding organic acid, similarly to the well characterized amidase from Rhodococcus rhodochrous J1 [2].
 

High impact information on gatA-3

  • Recombinant amidase is a 55.8 kDa enzyme from the thermophilic archaeon Sulfolobus solfataricus MT4 that catalyses the hydrolysis of aliphatic amides of 2-6 C atoms as well as many aromatic amides [3].
  • The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles. Ser195 and Cys145 are predicted to be the active site nucleophiles [2].
 

Analytical, diagnostic and therapeutic context of gatA-3

References

  1. Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus. d'Abusco, A.S., Ammendola, S., Scandurra, R., Politi, L. Extremophiles (2001) [Pubmed]
  2. The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles. Ser195 and Cys145 are predicted to be the active site nucleophiles. Cilia, E., Fabbri, A., Uriani, M., Scialdone, G.G., Ammendola, S. FEBS J. (2005) [Pubmed]
  3. Crystallization and X-ray diffraction measurements of a thermophilic archaeal recombinant amidase from Sulfolobus solfataricus MT4. Nastopoulos, V., Vallone, B., Politi, L., Scotto D'Abusco, A., Scandurra, R., Tsernoglou, D. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]
 
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