PMID:16990279
| Citation |
Kuznetsova, E, Proudfoot, M, Gonzalez, CF, Brown, G, Omelchenko, MV, Borozan, I, Carmel, L, Wolf, YI, Mori, H, Savchenko, AV, Arrowsmith, CH, Koonin, EV, Edwards, AM and Yakunin, AF (2006) Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J. Biol. Chem. 281:36149-61 |
|---|---|
| Abstract |
Haloacid dehalogenase (HAD)-like hydrolases are a vast superfamily of largely uncharacterized enzymes, with a few members shown to possess phosphatase, beta-phosphoglucomutase, phosphonatase, and dehalogenase activities. Using a representative set of 80 phosphorylated substrates, we characterized the substrate specificities of 23 soluble HADs encoded in the Escherichia coli genome. We identified small molecule phosphatase activity in 21 HADs and beta-phosphoglucomutase activity in one protein. The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. Rather than following the classical "one enzyme-one substrate" model, most of the E. coli HADs show remarkably broad and overlapping substrate spectra. At least 12 reactions catalyzed by HADs currently have no EC numbers assigned in Enzyme Nomenclature. Surprisingly, most HADs hydrolyzed small phosphodonors (acetyl phosphate, carbamoyl phosphate, and phosphoramidate), which also serve as substrates for autophosphorylation of the receiver domains of the two-component signal transduction systems. The physiological relevance of the phosphatase activity with the preferred substrate was validated in vivo for one of the HADs, YniC. Many of the secondary activities of HADs might have no immediate physiological function but could comprise a reservoir for evolution of novel phosphatases. |
| Links |
PubMed Online version:10.1074/jbc.M605449200 |
| Keywords |
Catalysis; Cloning, Molecular; Cluster Analysis; Computational Biology; Escherichia coli/genetics; Evolution, Molecular; Genome, Bacterial; Glucose/chemistry; Hydrolysis; Kinetics; Multigene Family; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphorylation; Signal Transduction; Substrate Specificity |
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The malachite green assay used by the authors to measure phosphatase activity is described in Baykov et al. (1988).[1] The paper cites Kuznetsova et al. 2005, which cites Baykov et al.
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