ArticleThe Journal of biological chemistry2012
Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Regioisomeric Family of Novel Fluorescent Substrates for SHIP2.ACS medicinal chemistry letters · 2020Article
- Article
- Characteristics of the First Protein Tyrosine Phosphatase with Phytase Activity from a Soil Metagenome.Genes · 2019Article
- Bacterial PhyA protein-tyrosine phosphatase-likeThe Journal of biological chemistry · 2017Article
- Article
- LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance.Protein science : a publication of the Protein Society · 2012Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-tyrosine phosphatase-like inositol polyphosphatases are microbial enzymes that catalyze the stepwise removal of one or more phosphates from highly phosphorylated myo-inositols via a relatively ordered pathway. To understand the substrate specificity and kinetic mechanism of these enzymes we have determined high resolution, single crystal, x-ray crystallographic structures of inactive Selenomonas ruminantium PhyA in complex with myo-inositol hexa- and pentakisphosphate. These structures provide the first glimpse of a myo-inositol polyphosphatase-ligand complex consistent with its known specificity and reveal novel features of the kinetic mechanism. To complement the structural studies, fluorescent binding assays have been developed and demonstrate that the K(d) for this enzyme is several orders of magnitude lower than the K(m). Together with rapid kinetics data, these results suggest that the protein tyrosine phosphatase-like inositol polyphosphatases have a two-step, substrate-binding mechanism that facilitates catalysis.
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Registered trials
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