Purcarea C, Simon V, Prieur D, Hervé G
Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, Université Pierre et Marie Curie, Paris, France.
Eur J Biochem. 1996 Feb 15;236(1):189-99. doi: 10.1111/j.1432-1033.1996.00189.x.
Carbamoyl-phosphate synthetase was purified from the deep-sea hyperthermophilic archaebacterium Pyrococcus abyssi. This enzyme appears to be monomeric and uses ammonium salts as nitrogen donor. Its activity is inhibited by some nucleotides that compete with ATP. In contrast with the carbamoyl-phosphate synthetases investigated so far, this enzyme is very resistant to high temperature. Its low molecular mass (46.6 kDa) and its catalytic properties suggest that the gene coding for this enzyme is a previously postulated ancestor, whose duplication gave the genes coding for carbamoyl-phosphate synthetases and carbamate kinases.
氨甲酰磷酸合成酶是从深海嗜热古细菌深渊热球菌中纯化得到的。这种酶似乎是单体形式，以铵盐作为氮供体。它的活性受到一些与ATP竞争的核苷酸的抑制。与迄今为止研究的氨甲酰磷酸合成酶不同，这种酶对高温具有很强的抗性。其低分子量（46.6 kDa）及其催化特性表明，编码这种酶的基因是先前推测的祖先基因，其复制产生了编码氨甲酰磷酸合成酶和氨基甲酸激酶的基因。
