A natural carbohydrate substrate for Mycobacterium tuberculosis methionine sulfoxide reductase A.
نویسندگان
چکیده
Enzymatic reduction of the methylsulfinylxylofuranosyl (MSX) groups in lipoarabinomannan provides proof of the absolute configuration of MSX and a possible biochemical mechanism for oxidative protection in Mycobacterium tuberculosis.
منابع مشابه
Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections i...
متن کاملComplex with Protein-Bound Methionine Methionine Sulfoxide Reductase A in Mycobacterium tuberculosis
متن کامل
Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates.
Inducible nitric oxide synthase (iNOS) plays an important role in host defense. Macrophages expressing iNOS release the reactive nitrogen intermediates (RNI) nitrite and S-nitrosoglutathione (GSNO), which are bactericidal in vitro at a pH characteristic of the phagosome of activated macrophages. We sought to characterize the active intrabacterial forms of these RNI and their molecular targets. ...
متن کامل5 - Adenosinephosphosulfate Lies at a Metabolic Branch
Bacterial sulfate assimilation pathways provide for activation of inorganic sulfur for the biosynthesis of cysteine and methionine, through either adenosine 5 phosphosulfate (APS) or 3 -phosphoadenosine 5 -phosphosulfate (PAPS) as intermediates. PAPS is also the substrate for sulfotransferases that produce sulfolipids, putative virulence factors, in Mycobacterium tuberculosis such as SL-1. In t...
متن کامل5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria.
Bacterial sulfate assimilation pathways provide for activation of inorganic sulfur for the biosynthesis of cysteine and methionine, through either adenosine 5'-phosphosulfate (APS) or 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as intermediates. PAPS is also the substrate for sulfotransferases that produce sulfolipids, putative virulence factors, in Mycobacterium tuberculosis such as SL-1. In ...
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ورودعنوان ژورنال:
- Chemical communications
دوره 1 شماره
صفحات -
تاریخ انتشار 2009