The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
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DOI：
10.1016/s0968-0004(03)00061-6
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发表时间：
2003-05-01
影响因子：
13.8
通讯作者：
Rawlings, ND
中科院分区：
文献类型：
--
作者：
Bateman, A;Rawlings, ND
肽聚糖的切割在细菌细胞分裂、细胞生长和细胞裂解中起重要作用。在这里，我们发现，几个已知的肽聚糖酰胺酶属于一个家庭，其中包括许多蛋白质的以前未知的功能。该家族包括两种不同的肽聚糖切割活性：L-胞壁酰-L-丙氨酸酰胺酶和D-丙氨酰-甘氨酰内肽酶活性。该家族包括来自细菌和致病性锥虫的双功能谷胱甘肽亚精胺合酶/酰胺酶的酰胺酶部分。谷胱甘肽异培脒合酶被认为是锥虫中保护免受氧自由基损伤的替代途径的关键组分，并已被提议作为潜在的药物靶点。半胱氨酸、组氨酸依赖性酰胺水解酶/肽酶（英语：amidohydrolases/peptidases）结构域通常与其他切割肽聚糖的结构域结合。大量的多功能水解酶表明，它们可能以合作的方式裂解专门的底物。
Cleavage of peptidoglycan plays an important role in bacterial cell division, cell growth and cell lysis. Here, we reveal that several known peptidoglycan amidases fall into a family, which includes many proteins of previously unknown function. The family includes two different peptidoglycan cleavage activities: L-Muramoyl-L-alanine amidase and D-alanyl-glycyl endopeptidase activity. The family includes the amidase portion of the bifunctional glutathionylspermidine synthase/amidase enzyme from bacteria and pathogenic trypanosomes. The glutathionyispermidine synthase is thought to be a key component of the alternative pathway in trypanosomes for protection from oxygen-radical damage and has been proposed as a potential drug target. The CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain is often found in association with other domains that cleave peptidoglycan. The large number of multifunctional hydrolases suggests that they might act in a cooperative manner to cleave specialized substrates.