Rottmann W H, Deselms K R, Niclas J, Camerato T, Holman P S, Green C J, Tolan D R
Biochimie. 1987 Feb;69(2):137-45. doi: 10.1016/0300-9084(87)90246-x.
The complete protein sequence of the human aldolase C isozyme has been determined from recombinant genomic clones. A genomic fragment of 6673 base pairs was isolated and the DNA sequence determined. Aldolase protein sequences, being highly conserved, allowed the derivation of the sequence of this isozyme by comparison of open reading frames in the genomic DNA to the protein sequence of other human aldolase enzymes. The protein sequence of the third aldolase isozyme found in vertebrates, aldolase C, completes the primary structural determination for this family of isozymes. Overall, the aldolase C isozyme shared 81% amino acid homology with aldolase A and 70% homology with aldolase B. The comparisons with other aldolase isozymes revealed several aldolase C-specific residues which could be involved in its function in the brain. The data indicated that the gene structure of aldolase C is the same as other aldolase genes in birds and mammals, having nine exons separated by eight introns, all in precisely the same positions, only the intron sizes being different. Eight of these exons contain the protein coding region comprised of 363 amino acids. The entire gene is approximately 4 kilobases.
人醛缩酶C同工酶的完整蛋白质序列已通过重组基因组克隆确定。分离出一个6673个碱基对的基因组片段并测定了其DNA序列。醛缩酶蛋白质序列高度保守，通过将基因组DNA中的开放阅读框与其他人醛缩酶的蛋白质序列进行比较，可推导该同工酶的序列。在脊椎动物中发现的第三种醛缩酶同工酶醛缩酶C的蛋白质序列，完成了该同工酶家族的一级结构测定。总体而言，醛缩酶C同工酶与醛缩酶A的氨基酸同源性为81%，与醛缩酶B的同源性为70%。与其他醛缩酶同工酶的比较揭示了几个醛缩酶C特异性残基，这些残基可能与其在大脑中的功能有关。数据表明，醛缩酶C的基因结构与鸟类和哺乳动物中的其他醛缩酶基因相同，有9个外显子被8个内含子隔开，所有外显子和内含子的位置完全相同，只是内含子大小不同。其中8个外显子包含由363个氨基酸组成的蛋白质编码区。整个基因约为4千碱基。
