ArticleProtein science : a publication of the Protein Society1999
Photoaffinity labeling probe for the substrate binding site of human phenol sulfotransferase (SULT1A1): 7-azido-4-methylcoumarin.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 34 citations in OpenAlex.
- A Photoalkylative Fluorogenic Probe of Guttiferone A for Live Cell Imaging and Proteome Labeling inMolecules (Basel, Switzerland) · 2020Article
- Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation.Archives of biochemistry and biophysics · 2011Article
- para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E[middle dot]PAP complex and reformation of E[middle dot]PAPS.The Journal of biological chemistry · 2009Article
- Sulfation of dietary flavonoids by human sulfotransferases.Xenobiotica; the fate of foreign compounds in biological systems · 2009Article
- Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase.Biochemistry · 2008Article
- Effect of folic acid on methotrexate induction of sulfotransferases in rats.Drug metabolism letters · 2008Article
- CYP2E1 active site residues in substrate recognition sequence 5 identified by photoaffinity labeling and homology modeling.Archives of biochemistry and biophysics · 2007Article
- Arginine residues in the active site of human phenol sulfotransferase (SULT1A1).The Journal of biological chemistry · 2003Article
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5 authors at 2 institutions in 1 country.
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Abstract
A novel fluorescent photoactive probe 7-azido-4-methylcoumarin (AzMC) has been characterized for use in photoaffinity labeling of the substrate binding site of human phenol sulfotransferase (SULT1A1 or P-PST-1). For the photoaffinity labeling experiments, SULT1A1 cDNA was expressed in Escherichia coli as a fusion protein to maltose binding protein (MBP) and purified to apparent homogeneity over an amylose column. The maltose moiety was removed by Factor Xa cleavage. Both MBSULT1A1 and SULT1A1 were efficiently photolabeled with AzMC. This labeling was concentration dependent. In the absence of light, AzMC competitively inhibited the sulfation of 4MU catalyzed by SULT1A1 (Ki = 0.47 +/- 0.05 mM). Moreover, enzyme activity toward 2-naphthol was inactivated in a time- and concentration-dependent manner. SULT1A1 inactivation by AzMC was protected by substrate but was not protected by cosubstrate. These results indicate that photoaffinity labeling with AzMC is highly suitable for the identification of the substrate binding site of SULT1A1. Further studies are aimed at identifying which amino acids modified by AzMC are localized in the binding site.
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