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Rv2607 from Mycobacterium tuberculosis Is a Pyridoxine 5′-Phosphate Oxidase with Unusual Substrate Specificity
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Rv2607 from Mycobacterium tuberculosis Is a Pyridoxine 5′-Phosphate Oxidase with Unusual Substrate Specificity
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Journal Article
Rv2607 from Mycobacterium tuberculosis Is a Pyridoxine 5′-Phosphate Oxidase with Unusual Substrate Specificity
2011
Overview
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.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ E coli
/ Enzymes
/ Flavin Mononucleotide - metabolism
/ Genomes
/ Genomics
/ Homology
/ Humans
/ Kinases
/ Kinetics
/ Medicine
/ Mycobacterium tuberculosis - enzymology
/ Oxidase
/ Oxidases
/ Proteins
/ Pyridoxal Phosphate - analogs & derivatives
/ Pyridoxal Phosphate - metabolism
