ArticleBiochemistry2011
Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Repurposing approved drugs targetingFrontiers in cellular and infection microbiology · 2026Article
- The Role of Quorum Sensing Molecules in Bacterial-Plant Interactions.Metabolites · 2023Review
- A bifunctional salvage pathway for two distinct S-adenosylmethionine by-products that is widespread in bacteria, including pathogenic Escherichia coli.Molecular microbiology · 2020Article
- Revisiting the methionine salvage pathway and its paralogues.Microbial biotechnology · 2019Article
- Leishmania infantum 5'-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target.BMC structural biology · 2017Article
- Microbial pathway for anaerobic 5'-methylthioadenosine metabolism coupled to ethylene formation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Tight binding enantiomers of pre-clinical drug candidates.Bioorganic & medicinal chemistry · 2015Article
- Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine.Journal of bacteriology · 2014Article
- Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa.Biochemistry · 2012Article
- Synthesis and evaluation of eight- and four-membered iminosugar analogues as inhibitors of testicular ceramide-specific glucosyltransferase, testicular β-glucosidase 2, and other glycosidases.The Journal of organic chemistry · 2012Article
- Identification of Rv0535 as methylthioadenosine phosphorylase from Mycobacterium tuberculosis.Tuberculosis (Edinburgh, Scotland) · 2012Article
- Identification and characterization of two adenosine phosphorylase activities in Mycobacterium smegmatis.Journal of bacteriology · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The PA3004 gene of Pseudomonas aeruginosa PAO1 was originally annotated as a 5'-methylthioadenosine phosphorylase (MTAP). However, the PA3004 encoded protein uses 5'-methylthioinosine (MTI) as a preferred substrate and represents the only known example of a specific MTI phosphorylase (MTIP). MTIP does not utilize 5'-methylthioadenosine (MTA). Inosine is a weak substrate with a k(cat)/K(m) value 290-fold less than MTI and is the second best substrate identified. The crystal structure of P. aeruginosa MTIP (PaMTIP) in complex with hypoxanthine was determined to 2.8 Å resolution and revealed a 3-fold symmetric homotrimer. The methylthioribose and phosphate binding regions of PaMTIP are similar to MTAPs, and the purine binding region is similar to that of purine nucleoside phosphorylases (PNPs). The catabolism of MTA in P. aeruginosa involves deamination to MTI and phosphorolysis to hypoxanthine (MTA → MTI → hypoxanthine). This pathway also exists in Plasmodium falciparum, where the purine nucleoside phosphorylase (PfPNP) acts on both inosine and MTI. Three tight-binding transition state analogue inhibitors of PaMTIP are identified with dissociation constants in the picomolar range. Inhibitor specificity suggests an early dissociative transition state for PaMTIP. Quorum sensing molecules are associated with MTA metabolism in bacterial pathogens suggesting PaMTIP as a potential therapeutic target.
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