ArticleJournal of bacteriology2001
The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica serovar Typhimurium possess distinct biochemical properties.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Predicting clinical outcome ofMicrobial genomics · 2025Article
- Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria.International journal of molecular sciences · 2024Article
- Manganese Utilization inFrontiers in cell and developmental biology · 2022Review
- Coordinate regulation of the expression of SdsR toxin and its downstream pphA gene by RyeA antitoxin in Escherichia coli.Scientific reports · 2019Article
- High-affinity manganese coordination by human calprotectin is calcium-dependent and requires the histidine-rich site formed at the dimer interface.Journal of the American Chemical Society · 2013Article
- Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case study.Metallomics : integrated biometal science · 2012Review
- Manganese binds to Clostridium difficile Fbp68 and is essential for fibronectin binding.The Journal of biological chemistry · 2011Article
- Myxococcus xanthus Pph2 is a manganese-dependent protein phosphatase involved in energy metabolism.The Journal of biological chemistry · 2009Article
- Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes.BMC evolutionary biology · 2004Article
- Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+).Journal of bacteriology · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salmonella enterica serovar Typhimurium requires Mn(2+), but only a few Mn(2+)-dependent enzymes have been identified from bacteria. To characterize Mn(2+)-dependent enzymes from serovar Typhimurium, two putative PPP-family protein phosphatase genes were cloned from serovar Typhimurium and named prpA and prpB. Their DNA-derived amino acid sequences showed 61% identity to the corresponding Escherichia coli proteins and 41% identity to each other. Each phosphatase was expressed in E. coli and purified to near electrophoretic homogeneity. Both PrpA and PrpB absolutely required a divalent metal for activity. As with other phosphatases of this class, Mn(2+) had the highest affinity and stimulated the greatest activity. The apparent K(a) of PrpA for Mn(2+) of 65 microM was comparable to that for other bacterial phosphatases, but PrpB had a much higher affinity for Mn(2+) (1.3 microM). The pH optima were pH 6.5 for PrpA and pH 8 for PrpB, while the optimal temperatures were 45 to 55 degrees C for PrpA and 30 to 37 degrees C for PrpB. Each phosphatase could hydrolyze phosphorylated serine, threonine, or tyrosine residues, but their relative specific activities varied with the specific substrate tested. These differences suggest that each phosphatase is used by serovar Typhimurium under different growth or environmental conditions such as temperature or acidity.
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