...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).
【24h】

Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).

机译：结构特性和动力学特性金黄色葡萄球菌的丙氨酸消旋酶(Mu50)。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Staphylococcus aureus is an opportunistic Gram-positive bacterium which causes a wide variety of diseases ranging from minor skin infections to potentially fatal conditions such as pneumonia, meningitis and septicaemia. The pathogen is a leading cause of nosocomial acquired infections, a problem that is exacerbated by the existence of methicillin- and glycopeptide antibiotic-resistant strains which can be challenging to treat. Alanine racemase (Alr) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes reversible racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of Alr is lethal to prokaryotes. Additionally, while ubiquitous amongst bacteria, this enzyme is absent in humans and most eukaryotes, making it an excellent antibiotic drug target. The crystal structure of S. aureus alanine racemase (Alr(Sas)), the sequence of which corresponds to that from the highly antibiotic-resistant Mu50 strain, has been solved to 2.15 A resolution. Comparison of the Alr(Sas) structure with those of various alanine racemases demonstrates a conserved overall fold, with the enzyme sharing most similarity to those from other Gram-positive bacteria. Structural examination indicates that the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design. Kinetic constants were calculated in this study and are reported here. The potential for a disulfide bond in this structure is noted. This structural and biochemical information provides a template for future structure-based drug-development efforts targeting Alr(Sas).
机译：金黄色葡萄球菌是一个机会革兰氏阳性细菌引起广泛各种各样的疾病从轻微的皮肤这种感染可能致命的条件肺炎、脑膜炎和败血症。病原体是院内的一个主要原因获得感染,这是一个问题甲氧西林的存在,加剧了糖肽抗生素耐药菌株,治疗可能是一个挑战。(规律)是一个pyridoxal-5 -phosphate-dependent酶催化可逆外消旋化丙氨酸对映体之间。细菌细胞壁的主要成分肽聚糖,抑制规律是致命的原核生物。在细菌中,这种酶在人类中缺席和大多数真核生物,成为一个优秀的抗生素药物的目标。金黄色葡萄球菌丙氨酸消旋酶(规律(Sas))这对应的序列高度耐药Mu50应变2.15解决方案来解决。规律(Sas)结构与各种丙氨酸消旋酶演示了一个守恒整体折叠,与酶分享最相似的从其他革兰氏阳性细菌。检查表明,活性部位绑定的口袋,二聚体界面和活性部位入口通道酶的潜在目标structure-aided抑制剂的设计。在这项研究中,计算了常量报告在这里。在这个结构。生化信息提供了一个模板未来基于结构的药物开发targeting空气(Sas)。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号