ArticleBiochemistry2011
Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
- Response regulator PorX coordinates oligonucleotide signalling and gene expression to control the secretion of virulence factors.Nucleic acids research · 2022Article
- Global and seasonal variation of marine phosphonate metabolism.The ISME journal · 2022Article
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.The Journal of biological chemistry · 2017Article
- Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily.Journal of the American Chemical Society · 2016Article
- Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Journal of the American Chemical Society · 2015Article
- Article
- The treatment-naive microbiome in new-onset Crohn's disease.Cell host & microbe · 2014Article
- Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation.Chemistry & biology · 2014Article
- Root traits and microbial community interactions in relation to phosphorus availability and acquisition, with particular reference to Brassica.Frontiers in plant science · 2014Review
- Site-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.Biochemistry · 2013Article
- Phosphonate biosynthesis and catabolism: a treasure trove of unusual enzymology.Current opinion in chemical biology · 2013Review
- Organophosphonates revealed: new insights into the microbial metabolism of ancient molecules.Nature reviews. Microbiology · 2013Review
- Cellular function and molecular structure of ecto-nucleotidases.Purinergic signalling · 2012Review
- Answers to the carbon-phosphorus lyase conundrum.Chembiochem : a European journal of chemical biology · 2012Article
- The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment.Frontiers in microbiology · 2012Article
- Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase.Chemistry & biology · 2011Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Phosphonates constitute a class of natural products that mimic the properties of the more common organophosphate ester metabolite yet are not readily degraded owing to the direct linkage of the phosphorus atom to the carbon atom. Phosphonate hydrolases have evolved to allow bacteria to utilize environmental phosphonates as a source of carbon and phosphorus. The work reported in this paper examines one such enzyme, phosphonoacetate hydrolase. By using a bioinformatic approach, we circumscribed the biological range of phosphonoacetate hydrolase to a select group of bacterial species from different classes of Proteobacteria. In addition, using gene context, we identified a novel 2-aminoethylphosphonate degradation pathway in which phosphonoacetate hydrolase is a participant. The X-ray structure of phosphonoformate-bound phosphonoacetate hydrolase was determined to reveal that this enzyme is most closely related to nucleotide pyrophosphatase/diesterase, a promiscuous two-zinc ion metalloenzyme of the alkaline phosphatase enzyme superfamily. The X-ray structure and metal ion specificity tests showed that phosphonoacetate hydrolase is also a two-zinc ion metalloenzyme. By using site-directed mutagenesis and (32)P-labeling strategies, the catalytic nucleophile was shown to be Thr64. A structure-guided, site-directed mutation-based inquiry of the catalytic contributions of active site residues identified Lys126 and Lys128 as the most likely candidates for stabilization of the aci-carboxylate dianion leaving group. A catalytic mechanism is proposed which combines Lys12/Lys128 leaving group stabilization with zinc ion activation of the Thr64 nucleophile and the substrate phosphoryl group.
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