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结核分枝杆菌 Rv2607 是一种吡啶酮 5'-磷酸氧化酶,具有不寻常的底物特异性。

Rv2607 from Mycobacterium tuberculosis is a pyridoxine 5'-phosphate oxidase with unusual substrate specificity.

机构信息

National Institute of Allergy and Infectious Disease, National Institutes of Health, Bethesda, Maryland, United States of America.

出版信息

PLoS One. 2011;6(11):e27643. doi: 10.1371/journal.pone.0027643. Epub 2011 Nov 14.

Abstract

Despite intensive effort, the majority of the annotated Mycobacterium tuberculosis genome consists of genes encoding proteins of unknown or poorly understood function. For example, there are seven conserved hypothetical proteins annotated as homologs of pyridoxine 5'-phosphate oxidase (PNPOx), an enzyme that oxidizes pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) to form pyridoxal 5'-phosphate (PLP). We have characterized the function of Rv2607 from Mycobacterium tuberculosis H37Rv and shown that it encodes a PNPOx that oxidizes PNP to PLP. The k(cat) and K(M) for this reaction were 0.01 s(-1) and 360 µM, respectively. Unlike many PNPOx enzymes, Rv2607 does not recognize PMP as a substrate.

摘要

尽管付出了巨大努力,大部分已注释的结核分枝杆菌基因组仍包含编码具有未知或功能理解有限的蛋白的基因。例如,有七个保守的假定蛋白被注释为吡哆醇 5'-磷酸氧化酶 (PNPOx) 的同源物,该酶将吡哆醇 5'-磷酸 (PNP) 或吡哆醛 5'-磷酸 (PMP) 氧化为吡哆醛 5'-磷酸 (PLP)。我们已经对结核分枝杆菌 H37Rv 中的 Rv2607 进行了功能表征,并表明它编码一种 PNPOx,可将 PNP 氧化为 PLP。该反应的 k(cat) 和 K(M) 值分别为 0.01 s(-1) 和 360 µM。与许多 PNPOx 酶不同,Rv2607 不识别 PMP 作为底物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed04/3215729/ef62034a97be/pone.0027643.g001.jpg

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