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.
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CITATION STYLE
Mashalidis, E. H., Mukherjee, T., Śledź, P., Matak-Vinković, D., Boshoff, H., Abell, C., & Barry, C. E. (2011). Rv2607 from mycobacterium tuberculosis is a pyridoxine 5′-phosphate oxidase with unusual substrate specificity. PLoS ONE, 6(11). https://doi.org/10.1371/journal.pone.0027643
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