脱羧
化学
基质(水族馆)
苯乙酸
羧基裂解酶
酶
立体化学
催化作用
生物化学
生物
生态学
作者
Qiang Lu,Yifeng Wei,Lianyun Lin,J. Y. Liu,Yongxu Duan,Yaxin Li,Weixiang Zhai,Yangping Liu,Ee Lui Ang,Huimin Zhao,Zhiguang Yuchi,Yan Zhang
标识
DOI:10.1021/acscatal.1c01253
摘要
The glycyl radical enzymes (GREs) p-hydroxyphenylacetate (HPA) decarboxylase (HPAD), indoleacetate decarboxylase, and phenylacetate decarboxylase catalyze the radical-mediated decarboxylation of arylacetates, which are products of bacterial aromatic amino acid fermentation. Here, we report the discovery and structural and biochemical investigation of a fourth GRE arylacetate decarboxylase (AAD) from Olsenella scatoligenes that catalyzes HPA decarboxylation. AAD also catalyzes the decarboxylation of p-aminophenylacetate, which is not a substrate of HPAD, and lacks the Fe–S cluster containing small subunit. The structure of AAD in complex with p-hydroxyphenylacetate was determined by X-ray crystallography. The differing substrate ranges and active site structures of AAD and HPAD suggest distinct catalytic mechanisms, underscoring the diversity of radical-mediated decarboxylation reactions.
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