Sauer J, Nygaard P
Department of Biological Chemistry, University of Copenhagen, 1307 Copenhagen K, Denmark.
J Bacteriol. 1999 Mar;181(6):1958-62. doi: 10.1128/JB.181.6.1958-1962.1999.
The hpt gene from the archaeon Methanobacterium thermoautotrophicum, encoding hypoxanthine (guanine) phosphoribosyltransferase, was cloned by functional complementation into Escherichia coli. The hpt-encoded amino acid sequence is most similar to adenine phosphoribosyltransferases, but the encoded enzyme has activity only with hypoxanthine and guanine. The synthesis of the recombinant enzyme is apparently limited by the presence of the rare arginine codons AGA and AGG and the rare isoleucine AUA codon on the hpt gene. The recombinant enzyme was purified to apparent homogeneity.
通过功能互补将来自嗜热自养甲烷杆菌的hpt基因克隆到大肠杆菌中,该基因编码次黄嘌呤(鸟嘌呤)磷酸核糖转移酶。hpt编码的氨基酸序列与腺嘌呤磷酸核糖转移酶最为相似,但所编码的酶仅对次黄嘌呤和鸟嘌呤具有活性。重组酶的合成显然受到hpt基因上稀有精氨酸密码子AGA和AGG以及稀有异亮氨酸AUA密码子的限制。重组酶被纯化至表观均一。