...
首页> 外文期刊>FEBS Letters >Nitrite reductase from Pseudomonas aeruginosa: Sequence of the gene and the protein
【24h】

Nitrite reductase from Pseudomonas aeruginosa: Sequence of the gene and the protein

机译:铜绿假单胞菌的亚硝酸盐还原酶:基因和蛋白质的序列

获取原文
   

获取外文期刊封面封底 >>

       

摘要

>The gene coding for nitrite reductase of Pseudomonas aeruginosa has been cloned and its sequence determined. The coding region is 1707 bp long and contains information for a polypeptide chain of 568 amino acids. The sequence of the mature protein has been confirmed independently by extensive amino acid sequencing. The amino-terminus of the mature protein is located at Lys-26; the preceding 25 residue long extension shows the features typical of signal peptides. Therefore the enzyme is probably secreted into the periplasmic space. The mature protein is made of 543 amino acid residues and has a molecular mass of 60204 Da. The c-heme-binding domain, which contains the only two Cys of the molecule, is located at the amino-terminal region. Analysis of the protein sequence in terms of hydrophobicity profile gives results consistent with the fact that the enzyme is fully water soluble and not membrane bound; the most hydrophilic region appears to correspond to the c-heme domain. Secondary structure predictions are in general agreement with previous analysis of circular dichroic data.
机译:>铜绿假单胞菌的亚硝酸还原酶编码基因已被克隆并确定了序列。编码区长1707 bp,包含568个氨基酸的多肽链信息。成熟蛋白质的序列已通过广泛的氨基酸测序独立确认。成熟蛋白的氨基末端位于Lys-26。前25个残基的长延伸显示了信号肽的典型特征。因此,该酶可能被分泌到周质空间中。成熟的蛋白质由543个氨基酸残基组成,分子量为60204 Da。 c -血红素结合域位于分子的氨基末端区域,该域仅含有分子的两个半胱氨酸。根据疏水性分析蛋白质序列可得出与酶完全溶于水而不与膜结合的事实相符的结果。最亲水的区域似乎对应于 c -血红素域。二级结构的预测与圆二色性数据的先前分析总体上是一致的。

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