Université Grenoble 1, Grenoble, France.
FEBS Lett. 2010 Oct 22;584(20):4357-60. doi: 10.1016/j.febslet.2010.09.037. Epub 2010 Sep 29.
In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT.
在所有通过芳香族氨基酸途径合成苯丙氨酸和/或酪氨酸的生物体中,都需要预苯酸氨基转移酶将预苯酸转化为芳香族氨基酸。在这些生物体中,编码这种酶的基因的身份仍然未知。谷氨酸/天冬氨酸-预苯酸氨基转移酶(PAT)是芳香族氨基酸途径中最后一种没有归属的酶。我们报告了拟南芥预苯酸氨基转移酶的纯化、质谱鉴定和生化特性。我们的数据表明,这种活性由原核型质体天冬氨酸氨基转移酶(At2g22250)承担。这代表了第一个编码 PAT 的基因的鉴定。