Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability.
The cDNA for human liver phenol-sulfating phenol sulfotransferase (P-PST) has been cloned and the active enzyme expressed in Cos cells and bacteria. Analysis of the sequence identified two cysteine residues, one of which is highly conserved in the phenol sulfotransferase gene family. Previous studies with the pure human liver enzyme suggested that the conserved cysteine may be involved in binding substrates. Bacterial expression of P-PST with the cysteine converted to a serine indicates that the cysteine is not essential for activity or substrate binding, however, the mutant enzyme is significantly more sensitive to thermal inactivation.
Department of Pharmacology, University of Alabama at Birmingham 35294.
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Falany
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Zhuang
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Falany
D000595:Amino Acid Sequence; D000818:Animals; D015239:Arylsulfotransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003545:Cysteine / Q000737:chemistry; D006801:Humans; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D016296:Mutagenesis; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature
D012694:Serine; D015239:Arylsulfotransferase; D003545:Cysteine