ArticleACS chemical biology2011
Discovery of a cytokinin deaminase.
Article in ACS chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Growth ofBiomolecules · 2026Article
- The Discovery ofACS catalysis · 2026Article
- On the Origin of Substrate Specificity of Enzymes from the Amidohydrolase Superfamily.Angewandte Chemie (International ed. in English) · 2026Article
- Cytidine deaminases catalyze the conversion ofScience advances · 2023Article
- Isolation and characterization marine bacteria capable of degrading lignin-derived compounds.PloS one · 2020Article
- Manipulation of cytokinin level in the ergot fungus Claviceps purpurea emphasizes its contribution to virulence.Current genetics · 2018Article
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.Biochimica et biophysica acta · 2015Review
- Function discovery and structural characterization of a methylphosphonate esterase.Biochemistry · 2015Article
- Biochemical Characterization of Putative Adenylate Dimethylallyltransferase and Cytokinin Dehydrogenase from Nostoc sp. PCC 7120.PloS one · 2015Article
- Prediction of substrates for glutathione transferases by covalent docking.Journal of chemical information and modeling · 2014Article
- Structure-guided discovery of new deaminase enzymes.Journal of the American Chemical Society · 2013Article
- Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes.Biochemistry · 2013Article
- Assignment of pterin deaminase activity to an enzyme of unknown function guided by homology modeling and docking.Journal of the American Chemical Society · 2013Article
- Statistical potential for modeling and ranking of protein-ligand interactions.Journal of chemical information and modeling · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
An enzyme of unknown function within the amidohydrolase superfamily was discovered to catalyze the hydrolysis of N-6-substituted adenine derivatives, several of which are cytokinins. Cytokinins are a common type of plant hormone and N-6-substituted adenines are also found as modifications to tRNA. Patl2390, from Pseudoalteromonas atlantica T6c, was shown to hydrolytically deaminate N-6-isopentenyladenine to hypoxanthine and isopentenylamine with a k(cat)/K(m) of 1.2 × 10(7) M(-1) s(-1). Additional substrates include N-6-benzyl adenine, cis- and trans-zeatin, kinetin, O-6-methylguanine, N-6-butyladenine, N-6-methyladenine, N,N-dimethyladenine, 6-methoxypurine, 6-chloropurine, and 6-thiomethylpurine. This enzyme does not catalyze the deamination of adenine or adenosine. A comparative model of Patl2390 was computed using the three-dimensional crystal structure of Pa0148 (PDB code 3PAO ) as a structural template, and docking was used to refine the model to accommodate experimentally identified substrates. This is the first identification of an enzyme that will hydrolyze an N-6-substituted side chain larger than methylamine from adenine.
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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.