ArticleBiochemistry2012
Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Radiotolerant endophytic bacteria and analysis of the effects ofBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Article
- Aminofutalosine Deaminase in the Menaquinone Pathway ofBiochemistry · 2021Article
- 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
- 5'-Methylthioadenosine and Cancer: old molecules, new understanding.Journal of Cancer · 2019Review
- A simplified characterization ofChemical science · 2017Article
- 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
- Butremycin, the 3-hydroxyl derivative of ikarugamycin and a protonated aromatic tautomer of 5'-methylthioinosine from a Ghanaian Micromonospora sp. K310.Marine drugs · 2014Article
- Structure-guided discovery of new deaminase enzymes.Journal of the American Chemical Society · 2013Article
- Transition States, analogues, and drug development.ACS chemical biology · 2013Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa possesses an unusual pathway for 5'-methylthioadenosine (MTA) metabolism involving deamination to 5'-methylthioinosine (MTI) followed by N-ribosyl phosphorolysis to hypoxanthine and 5-methylthio-α-d-ribose 1-phosphate. The specific MTI phosphorylase of P. aeruginosa has been reported [Guan, R., Ho, M. C., Almo, S. C., and Schramm, V. L. (2011) Biochemistry 50, 1247-1254], and here we characterize MTA deaminase from P. aeruginosa (PaMTADA). Genomic analysis indicated the PA3170 locus to be a candidate for MTA deaminase (MTADA). Protein encoded by PA3170 was expressed and shown to deaminate MTA with 40-fold greater catalytic efficiency for MTA than for adenosine. The k(cat)/K(m) value of 1.6 × 10(7) M(-1) s(-1) for MTA is the highest catalytic efficiency known for an MTA deaminase. 5'-Methylthiocoformycin (MTCF) is a 4.8 pM transition state analogue for PaMTADA but causes no significant inhibition of human adenosine deaminase or MTA phosphorylase. MTCF is permeable to P. aeruginosa and exhibits an IC(50) of 3 nM on cellular PaMTADA activity. PaMTADA is the only activity in P. aeruginosa extracts to act on MTA. MTA and 5-methylthio-α-d-ribose are involved in quorum sensing pathways; thus, PaMTADA is a potential target for quorum sensing. The crystal structure of PaMTADA in complex with MTCF shows the transition state mimic 8(R)-hydroxyl group in contact with a catalytic site Zn(2+), the 5'-methylthio group in a hydrophobic pocket, and the transition state mimic of the diazepine ring in contact with a catalytic site Glu.
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Registered trials
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