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Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme
Chen, P.; Van Vliet, F.; Van de Casteele, M.; Legrain, C.; Cunin, R.; Glansdorff, N. (1998). Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme. J. Bacteriol. 180(23): 6389-6391
In: Journal of Bacteriology. American Society of Microbiology: Washington DC. ISSN 0021-9193; e-ISSN 1098-5530
Peer reviewed article  
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Auteurs  Top 
  • Chen, P.
  • Van Vliet, F.
  • Van de Casteele, M.
  • Legrain, C.
  • Cunin, R.
  • Glansdorff, N.
Abstract
    In the allosteric aspartate transcarbamylase (ATCase) from the hyperthermophilic eubacterium Thermotoga maritima, the catalytic and regulatory functions, which in class B ATCases are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers. The ATCases from T. maritima and Treponema denticola present intriguing similarities, suggesting horizontal gene transfer.
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