...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa
【24h】

Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa

机译：甲基噻吩诺酸肽在假单胞菌铜绿假单胞菌的替代法定传感途径中

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

Pseudomonas aeruginosa possesses an unusual pathway for 5′-methylthioadenosine (MTA) metabolism involving deamination to 5′-methylthioinosine (MTI) followed by N-ribosyl phosphorolysis to hypoxanthine and 5-methylthio-α-d-ribose 1-phosphate. The specific MTI phosphorylase of P. aeruginosa has been reported [Guan, R., Ho, M. C., Almo, S. C., and Schramm, V. L. (2011) Biochemistry 50, 1247-1254], and here we characterize MTA deaminase from P. aeruginosa (PaMTADA). Genomic analysis indicated the PA3170 locus to be a candidate for MTA deaminase (MTADA). Protein encoded by PA3170 was expressed and shown to deaminate MTA with 40-fold greater catalytic efficiency for MTA than for adenosine. The k _(cat)/K _m value of 1.6 × 10 ~7 M ~(-1) s ~(-1) for MTA is the highest catalytic efficiency known for an MTA deaminase. 5′-Methylthiocoformycin (MTCF) is a 4.8 pM transition state analogue for PaMTADA but causes no significant inhibition of human adenosine deaminase or MTA phosphorylase. MTCF is permeable to P. aeruginosa and exhibits an IC _(50) of 3 nM on cellular PaMTADA activity. PaMTADA is the only activity in P. aeruginosa extracts to act on MTA. MTA and 5-methylthio-α-d-ribose are involved in quorum sensing pathways; thus, PaMTADA is a potential target for quorum sensing. The crystal structure of PaMTADA in complex with MTCF shows the transition state mimic 8(R)-hydroxyl group in contact with a catalytic site Zn ~(2+), the 5′-methylthio group in a hydrophobic pocket, and the transition state mimic of the diazepine ring in contact with a catalytic site Glu.
机译：Pseudomonas铜绿假单胞菌具有5'-甲基硫核苷酸（MTA）代谢的不寻常的途径，涉及脱氨至5'-甲基硫氨酸（MTI），然后是N-核糖基磷解物与次黄嘌呤和5-甲基硫基-α-D-核糖1-磷酸盐。据报道了P.铜绿假单胞菌的特异性MTI磷酸化酶[关，R.，HO，MC，Almo，SC和Schramm，VL（2011）生物化学50,1247-1254]，以及来自P. Aeruginosa的MTA deaminase （帕姆图塔）。基因组分析表明PA3170基因座是MTA脱氨酶（MTADA）的候选者。 PA3170编码的蛋白质被表达并显示为脱氨酸MTA，对于MTA的催化效率为40倍，而不是腺苷。 MTA的1.6×10〜7m〜（-1）S〜（-1）的K _（猫）/ k _m值是MTA脱氨酶已知的最高催化效率。 5'-甲基硫代霉素（MTCF）是PAMTADA的4.8 PM过渡状态类似物，但不会显着抑制人腺苷脱氨酶或MTA磷酸化酶。 MTCF可透气至铜绿假单胞菌，并在细胞庞大的活动上表现出3nm的IC _（50）。 Pamtada是P.铜绿假单胞菌提取物的唯一活性，以对MTA采取行动。 MTA和5-甲基硫胺-α-D-核糖参与批量传感途径;因此，Pamtada是批量传感的潜在目标。与MTCF复合物的PAMTADA的晶体结构表明，疏水性袋中的5'-甲基硫基，5'-甲基硫基组接触的过渡状态模拟8（R） - 羟基，和过渡状态模拟与催化部位Glu接触的二氮堇环。

著录项

  • 来源
    《Biochemistry》 |2012年第45期|共10页
  • 作者

    Guan R.; Ho M.-C.; Fr?hlich R.F.G.; Tyler P.C.; Almo S.C.; Schramm V.L.;

  • 作者单位

    Department of Biochemistry Albert Einstein College of Medicine Yeshiva University 1300 Morris Park Avenue Bronx NY 10461 United States;

    Department of Biochemistry Albert Einstein College of Medicine Yeshiva University 1300 Morris Park Avenue Bronx NY 10461 United States;

    Carbohydrate Chemistry Team Industrial Research Ltd. Lower Hutt New Zealand;

    Carbohydrate Chemistry Team Industrial Research Ltd. Lower Hutt New Zealand;

    Department of Biochemistry Albert Einstein College of Medicine Yeshiva University 1300 Morris Park Avenue Bronx NY 10461 United States;

    Department of Biochemistry Albert Einstein College of Medicine Yeshiva University 1300 Morris Park Avenue Bronx NY 10461 United States;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

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