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嗜热栖热菌(Thermotoga maritima)中编码二氢叶酸还原酶的基因dyrA。

The dihydrofolate reductase-encoding gene dyrA of the hyperthermophilic bacterium Thermotoga maritima.

作者信息

Van de Casteele M, Legrain C, Wilquet V, Glansdorff N

机构信息

Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Belgium.

出版信息

Gene. 1995 May 26;158(1):101-5. doi: 10.1016/0378-1119(95)00090-s.

DOI:10.1016/0378-1119(95)00090-s
PMID:7789791
Abstract

The structural gene (dyrA) encoding dihydrofolate reductase (DHFR) of Thermotoga maritima has been cloned, sequenced and expressed in Escherichia coli. The dyrA gene, located immediately upstream from the gene encoding aspartate carbamoyltransferase (pyrB), encodes a highly thermostable enzyme with a distinct thermophilic activity profile. Important structural features are conserved among all bacterial DHFR, yet the DHFR of T. maritima appears unique in a number of insertions and deletions, some of which are reminiscent of eukaryotic DHFR.

摘要

嗜热栖热菌二氢叶酸还原酶(DHFR)的结构基因(dyrA)已被克隆、测序并在大肠杆菌中表达。dyrA基因位于天冬氨酸氨甲酰转移酶(pyrB)编码基因的紧邻上游,编码一种具有独特嗜热活性谱的高度耐热酶。所有细菌DHFR中都保守着重要的结构特征,但嗜热栖热菌的DHFR在一些插入和缺失方面显得独特,其中一些让人联想到真核生物的DHFR。

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Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme.来自嗜热真细菌海栖热袍菌的天冬氨酸转氨甲酰酶:融合的催化和调节多肽形成一种别构酶。
J Bacteriol. 1998 Dec;180(23):6389-91. doi: 10.1128/JB.180.23.6389-6391.1998.