ArticleBiochemistry2011
Pa0148 from Pseudomonas aeruginosa catalyzes the deamination of adenine.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Coupled-enzyme assay for MTAP activity in biological samples.Analytical biochemistry · 2026Article
- Anti-Inflammatory Metabolites in the Pathogenesis of Bacterial Infection.Frontiers in cellular and infection microbiology · 2022Review
- Biochemical Characterization ofFrontiers in bioengineering and biotechnology · 2018Article
- Gene Duplication in Pseudomonas aeruginosa Improves Growth on Adenosine.Journal of bacteriology · 2017Article
- Function discovery and structural characterization of a methylphosphonate esterase.Biochemistry · 2015Article
- Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes.Biochemistry · 2013Article
- Functional annotation and three-dimensional structure of an incorrectly annotated dihydroorotase from cog3964 in the amidohydrolase superfamily.Biochemistry · 2013Article
- Structure-based function discovery of an enzyme for the hydrolysis of phosphorylated sugar lactones.Biochemistry · 2012Article
- Discovery of a cytokinin deaminase.ACS chemical biology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Four proteins from NCBI cog1816, previously annotated as adenosine deaminases, have been subjected to structural and functional characterization. Pa0148 (Pseudomonas aeruginosa PAO1), AAur1117 (Arthrobacter aurescens TC1), Sgx9403e, and Sgx9403g have been purified and their substrate profiles determined. Adenosine is not a substrate for any of these enzymes. All of these proteins will deaminate adenine to produce hypoxanthine with k(cat)/K(m) values that exceed 10(5) M(-1) s(-1). These enzymes will also accept 6-chloropurine, 6-methoxypurine, N-6-methyladenine, and 2,6-diaminopurine as alternate substrates. X-ray structures of Pa0148 and AAur1117 have been determined and reveal nearly identical distorted (β/α)(8) barrels with a single zinc ion that is characteristic of members of the amidohydrolase superfamily. Structures of Pa0148 with adenine, 6-chloropurine, and hypoxanthine were also determined, thereby permitting identification of the residues responsible for coordinating the substrate and product.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.