Jackson F R
J Mol Evol. 1990 Oct;31(4):325-9. doi: 10.1007/BF02101126.
A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including Drosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.
一项数据库搜索揭示了原核生物和真核生物中依赖磷酸吡哆醛（PLP）的脱羧酶之间存在显著且广泛的序列相似性，其中包括果蝇谷氨酸脱羧酶（GAD）和细菌组氨酸脱羧酶（HDC）。基于这些发现，来自五个不同生物体的七种依赖PLP的脱羧酶序列已进行比对，以得出该酶家族的共有序列。此外，已采用定量方法来计算构成该家族的成对脱羧酶之间的相对进化距离。多重序列分析与定量结果强烈表明，所有依赖PLP的脱羧酶都有一个古老且共同的起源。该分析还表明，原核生物和真核生物的HDC活性是独立进化的。最后，一种灵敏的搜索算法（PROFILE）未能在蛋白质序列数据库中检测到该脱羧酶家族的其他成员。
