Vijayakumar S, Salerno J C
Department of Biology, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Biochim Biophys Acta. 1992 Dec 28;1160(3):281-6. doi: 10.1016/0167-4838(92)90089-v.
Sequence-alignment studies of the bovine mitochondrial cholesterol side-chain cleavage enzyme cytochrome P-450scc with the bacterial cytochrome P-450cam (camphor hydroxylating enzyme) have been undertaken. Our novel alignment of the sequences revealed 69 identical residues and many highly conserved regions. The results of the sequence alignment studies were used to model the 3-D structure of P-450scc based on the available crystal structure of P-450cam. The major insertions in the sequence are found mainly on four external-loop regions of the molecule, while the core structure of P-450cam is retained with subtle internal modifications. The most hydrophobic of these four external loops is proposed as a candidate for membrane attachment.
已对牛线粒体胆固醇侧链裂解酶细胞色素P - 450scc与细菌细胞色素P - 450cam（樟脑羟化酶）进行了序列比对研究。我们对这些序列进行的新颖比对揭示了69个相同残基以及许多高度保守区域。序列比对研究的结果被用于基于细胞色素P - 450cam的现有晶体结构对细胞色素P - 450scc的三维结构进行建模。序列中的主要插入片段主要位于该分子的四个外环区域，而细胞色素P - 450cam的核心结构得以保留，但有细微的内部修饰。这四个外环中最疏水的一个被认为是膜附着的候选区域。
