flavin-adenine-dinucleotide and Streptococcal-Infections

flavin-adenine-dinucleotide has been researched along with Streptococcal-Infections* in 1 studies

Other Studies

1 other study(ies) available for flavin-adenine-dinucleotide and Streptococcal-Infections

ArticleYear
Myosin cross-reactive antigen of Streptococcus pyogenes M49 encodes a fatty acid double bond hydratase that plays a role in oleic acid detoxification and bacterial virulence.
    The Journal of biological chemistry, 2010, Apr-02, Volume: 285, Issue:14

    The myosin cross-reactive antigen (MCRA) protein family is highly conserved among different bacterial species ranging from Gram-positive to Gram-negative bacteria. Besides their ubiquitous occurrence, knowledge about the biochemical and physiological function of MCRA proteins is scarce. Here, we show that MCRA protein from Streptococcus pyogenes M49 is a FAD enzyme, which acts as hydratase on (9Z)- and (12Z)-double bonds of C-16, C-18 non-esterified fatty acids. Products are 10-hydroxy and 10,13-dihydroxy fatty acids. Kinetic analysis suggests that FAD rather stabilizes the active conformation of the enzyme and is not directly involved in catalysis. Analysis of S. pyogenes M49 grown in the presence of either oleic or linoleic acid showed that 10-hydroxy and 10,13-dihydroxy derivatives were the only products. No further metabolism of these hydroxy fatty acids was detected. Deletion of the hydratase gene caused a 2-fold decrease in minimum inhibitory concentration against oleic acid but increased survival of the mutant strain in whole blood. Adherence and internalization properties to human keratinocytes were reduced in comparison with the wild type. Based on these results, we conclude that the previously identified MCRA protein can be classified as a FAD-containing double bond hydratase, within the carbon-oxygen lyase family, that plays a role in virulence of at least S. pyogenes M49.

    Topics: Amino Acid Sequence; Cell Survival; Cross Reactions; Flavin-Adenine Dinucleotide; Gas Chromatography-Mass Spectrometry; Humans; Hydro-Lyases; Keratinocytes; Molecular Sequence Data; Mutation; Myosins; Oleic Acid; Phylogeny; Recombinant Proteins; Sequence Homology, Amino Acid; Streptococcal Infections; Streptococcus pyogenes; Virulence; Virulence Factors

2010