Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases
Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases
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DOI：
10.1016/s0968-0004(03)00062-8
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发表时间：
2003-05-01
影响因子：
13.8
通讯作者：
Galperin, MY
中科院分区：
文献类型：
--
作者：
Rigden, DJ;Jedrzejas, MJ;Galperin, MY
已经发现几种噬菌体编码的肽聚糖水解酶与多种细菌自溶素（N-乙酰胞壁酰-L-丙氨酸酰胺酶）、细菌和真核谷胱甘肽亚精胺酰胺酶、γ-D-谷氨酰-L-二氨基酸内肽酶和NLP/P60家族蛋白共享保守的酰胺酶结构域。所有这些蛋白质都含有保守的半胱氨酸和组氨酸残基，并水解含γ-谷氨酰的底物。这些半胱氨酸残基已被证明是必不可少的几个这些酰胺酶的活性和它们的硫醇基团显然作为亲核试剂的催化机制中的所有酶含有这个域。半胱氨酸、组氨酸依赖性酰胺水解酶/肽酶超家族包括多种以前未表征的蛋白质，包括噬菌体λ的尾部组装蛋白K。该超家族的一些成员是病原菌中重要的表面抗原，并且可能代表药物和/或疫苗靶点。
Several phage-encoded peptidoglycan hydrolases have been found to share a conserved amidase domain with a variety of bacterial autolysins (N-acetylmuramoyl-L-alanine amidases), bacterial and eukaryotic glutathionylspermidine amidases, gamma-D-glutamyl-L-diamino acid endopeptidase and NLP/P60 family proteins. All these proteins contain conserved cysteine and histidine residues and hydrolyze gamma-glutamyl-containing substrates. These cysteine residues have been shown to be essential for activity of several of these amidases and their thiol groups apparently function as the nucleophiles in the catalytic mechanisms of all enzymes containing this domain. The CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) superfamily includes a variety of previously uncharacterized proteins, including the tail assembly protein K of phage lambda. Some members of this superfamily are important surface antigens in pathogenic bacteria and might represent drug and/or vaccine targets.