Eubacterial arylamine N-acetyltransferases -: identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine and aspartate residues
Eubacterial arylamine N-acetyltransferases -: identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine and aspartate residues
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DOI：
10.1099/00221287-147-5-1137
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发表时间：
2001-05-01
期刊：
影响因子：
2.8
通讯作者：
Sim, E
中科院分区：
文献类型：
--
作者：
Payton, M;Mushtaq, A;Sim, E
芳胺N-乙酰基转移酶（NAT）是参与一系列芳胺和肼基异生物质的解毒的酶。NAT在真核生物中参与了对氨基苯甲酰谷氨酸的内源性代谢，但对NAT在原核生物中的分布和功能知之甚少。利用DNA文库筛选技术和全基因组测序数据的分析，我们已经确定了18个从变形菌和厚壁菌的nat样序列。最近，来自细菌鼠伤寒沙门氏菌（PDB登录号1 E2 T）的NAT的三维结构被解析，并揭示了由Cys（69）-His（107）-Asp（122）组成的活性位点催化三联体。这些残基在所有原核和真核NAT同源物中都是保守的，并且在活性位点三联体附近发现了三个高度保守的区域。据预测，原核NAT，基因簇的组成和基因组之间的分布，参与代谢的外源性物质来源于有机材料的分解。
Arylamine N-acetyltransferases (NATs) are enzymes involved in the detoxification of a range of arylamine and hydrazine-based xenobiotics. NATs have been implicated in the endogenous metabolism of p-aminobenzoyl glutamate in eukaryotes, although very little is known about the distribution and function of NAT in the prokaryotic kingdom. Using DNA library screening techniques and the analysis of data from whole-genome sequencing projects, we have identified 18 nat-like sequences from the Proteobacteria and Firmicutes. Recently, the three-dimensional structure of NAT derived from the bacterium Salmonella typhimurium (PDB accession code 1E2T) was resolved and revealed an active site catalytic triad composed of Cys(69)-His(107)-Asp(122). These residues have been shown to be conserved in all prokaryotic and eukaryotic NAT homologues together with three highly conserved regions which are found proximal to the active site triad, The characterization of prokaryotic NATs and NAT-like enzymes is reported. It is also predicted that prokaryotic NATs, based on gene cluster composition and distribution amongst genomes, participate in the metabolism of xenobiotics derived from decomposition of organic materials.