嗜肺军团菌
转氨酶
生物化学
磷酸吡哆醛
吡哆醛
酶
活动站点
化学
柠檬酸合酶
天冬氨酸转氨酶
转移酶
生物
立体化学
辅因子
细菌
碱性磷酸酶
遗传学
作者
Yong‐Shan Gao,Xin Yang,Hua Liao,Ming Wang,Qing Ge,Weiqiang Wang,Na Wang,Jinming Ma,Honghua Ge
标识
DOI:10.1016/j.bbrc.2023.149230
摘要
Legionella pneumophila aspartate aminotransferase (Lpg0070) is a member of the transaminase and belongs to the pyridoxal 5′-phosphate (PLP)-dependent superfamily. It is responsible for the transfer of α-amino between aspartate and α-ketoglutarate to form glutamate and oxaloacetate. Here, we report the crystal structure of Lpg0070 at the resolution of 2.14 Å and 1.7 Å, in apo-form and PLP-bound, respectively. Our structural analysis revealed the specific residues involved in the PLP binding and free form against PLP-bound supported conformational changes before substrate recognition. In vitro enzyme activity proves that the absence of the N-terminal arm reduces the enzyme activity of Lpg0070. These data provide further evidence to support the N-terminal arm plays a crucial role in catalytic activity.
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