Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme.
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ABSTRACT:
SUBMITTER: Chen P
PROVIDER: S-EPMC107728 | biostudies-literature | 1998 Dec
REPOSITORIES: biostudies-literature
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Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme.
Chen P P Van Vliet F F Van De Casteele M M Legrain C C Cunin R R Glansdorff N N
Journal of bacteriology 19981201 23
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. ...[more]
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