Dehydroepiandrosterone sulphate sulphoydrolase from human placenta microsomes—Properties of the purified enzyme

Gniot-Szulzycka, J

doi:10.1016/j.jsbmb.2005.11.008

Cited by 2 publications

(1 citation statement)

References 57 publications

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“…Nevertheless, it is evident that isoenzymes of steroid sulphohydrolase with more selective or absolute substrate preference exist [3][4][5][6][7][8][9]. Alternative expression of distinct exons of the gene or diverse posttranslational modifications may explain the existence of distinct forms of STS with different biological activity (substrate specificity) and subcellular localization.…”

Section: Introductionmentioning

confidence: 99%

Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane

Roszek

Gniot-Szulzycka

2008

The Journal of Steroid Biochemistry and Molecular Biology

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Section: Introductionmentioning

confidence: 99%

Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane

Roszek

Gniot-Szulzycka

2008

The Journal of Steroid Biochemistry and Molecular Biology

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Identification of zebrafish steroid sulfatase and comparative analysis of the enzymatic properties with human steroid sulfatase

Kurogi

Yoshihama

Williams

et al. 2019

The Journal of Steroid Biochemistry and Molecular Biology

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Steroid sulfatase (STS) plays an important role in the regulation of steroid hormones. Metabolism of steroid hormones in zebrafish has been investigated, but the action of steroid sulfatase remains unknown. In this study, a zebrafish sts was cloned, expressed, purified, and characterized in comparison with the orthologous human enzyme. Enzymatic assays demonstrated that similar to human STS, zebrafish Sts was most active in catalyzing the hydrolysis of estrone-sulfate and estradiol-sulfate, among five steroid sulfates tested as substrates. Kinetic analyses revealed that the K values of zebrafish Sts and human STS differed with respective substrates, but the catalytic efficiency as reflected by the V/K appeared comparable, except for DHEA-sulfate with which zebrafish Sts appeared less efficient. While zebrafish Sts was catalytically active at 28 °C, the enzyme appeared more active at 37 °C and with similar K values to those determined at 28 °C. Assays performed in the presence of different divalent cations showed that the activities of both zebrafish and human STSs were stimulated by Ca, Mg, and Mn, and inhibited by Zn and Fe. EMATE and STX64, two known mammalian steroid sulafatase inhibitors, were shown to be capable of inhibiting the activity of zebrafish Sts. Collectively, the results obtained indicated that zebrafish Sts exhibited enzymatic characteristics comparable to the human STS, suggesting that the physiological function of STS may be conserved between zebrafish and humans.

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Dehydroepiandrosterone sulphate sulphoydrolase from human placenta microsomes—Properties of the purified enzyme

Cited by 2 publications

References 57 publications

Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane

Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane

Identification of zebrafish steroid sulfatase and comparative analysis of the enzymatic properties with human steroid sulfatase

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