Skalnik D G, Simoni R D
DNA. 1985 Dec;4(6):439-44. doi: 10.1089/dna.1985.4.439.
We have determined the nucleotide sequence of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase cDNA. Comparison of the deduced amino acid sequence with the homologous sequence from Chinese hamster reveals highly conserved domains which appear to have functional significance. The amino-terminal membrane domain of HMG-CoA reductase exhibits 100% homology. This region may span the endoplasmic reticulum seven times and is thought to be involved in the sterol-regulated degradation of HMG-CoA reductase (Gil et al., 1985; Liscum et al., 1985). The carboxyl terminus contains the active site of the enzyme and exhibits greater than 99% homology. A central region linking these two conserved domains exhibits greater divergence. In this region there is only 85% homology between the two hamster lines, suggesting that this linkage domain has a less stringent structural requirement.
我们已经测定了叙利亚仓鼠3-羟基-3-甲基戊二酰辅酶A（HMG-CoA）还原酶cDNA的核苷酸序列。将推导的氨基酸序列与中国仓鼠的同源序列进行比较，发现高度保守的结构域似乎具有功能意义。HMG-CoA还原酶的氨基末端膜结构域表现出100%的同源性。该区域可能七次跨越内质网，被认为参与HMG-CoA还原酶的固醇调节降解（吉尔等人，1985年；利斯科姆等人，1985年）。羧基末端包含该酶的活性位点，表现出大于99%的同源性。连接这两个保守结构域的中央区域表现出更大的差异。在这个区域，两个仓鼠品系之间只有85%的同源性，这表明这个连接结构域的结构要求不太严格。
