A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis | |
Yu, Yamei ; Liang, Yu-He ; Brostromer, Erik ; Quan, Jun-Min ; Panjikar, Santosh ; Dong, Yu-Hui ; Su, Xiao-Dong | |
刊名 | journal of biological chemistry |
2006 | |
关键词 | HISTIDINE AMMONIA-LYASE COLI CYTOSINE DEAMINASE UROCANIC ACID DEGRADATION CRYSTALLIZATION DICTIONARY METABOLISM ENZYMES CLONING HUT |
DOI | 10.1074/jbc.M607703200 |
英文摘要 | Imidazolonepropionase (EC 3.5.2.7) catalyzes the third step in the universal histidine degradation pathway, hydrolyzing the carbon-nitrogen bonds in 4-imidazolone-5-propionic acid to yield N-formimino-L-glutamic acid. Here we report the crystal structures of the Bacillus subtilis imidazolonepropionase and its complex at 2.0-A resolution with substrate analog imidazole-4-acetic acid sodium (I4AA). The structure of the native enzyme contains two domains, a TIM (triose-phosphate isomerase) barrel domain with two insertions and a small beta-sandwich domain. The TIM barrel domain is quite similar to the members of the alpha/beta barrel metallo-dependent hydrolase superfamily, especially to Escherichia coli cytosine deaminase. A metal ion was found in the central cavity of the TIM barrel and was tightly coordinated to residues His-80, His-82, His-249, Asp-324, and a water molecule. X-ray fluorescence scan analysis confirmed that the bound metal ion was a zinc ion. An acetate ion, 6 A away from the zinc ion, was also found in the potential active site. In the complex structure with I4AA, a substrate analog, I4AA replaced the acetate ion and contacted with Arg-89, Try-102, Tyr-152, His-185, and Glu-252, further defining and confirming the active site. The detailed structural studies allowed us to propose a zinc-activated nucleophilic attack mechanism for the hydrolysis reaction catalyzed by the enzyme.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000242220800052&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; SCI(E); EI; PubMed; 10; ARTICLE; 48; 36929-36936; 281 |
语种 | 英语 |
内容类型 | 期刊论文 |
源URL | [http://ir.pku.edu.cn/handle/20.500.11897/345754] |
专题 | 生命科学学院 |
推荐引用方式 GB/T 7714 | Yu, Yamei,Liang, Yu-He,Brostromer, Erik,et al. A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis[J]. journal of biological chemistry,2006. |
APA | Yu, Yamei.,Liang, Yu-He.,Brostromer, Erik.,Quan, Jun-Min.,Panjikar, Santosh.,...&Su, Xiao-Dong.(2006).A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis.journal of biological chemistry. |
MLA | Yu, Yamei,et al."A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis".journal of biological chemistry (2006). |
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