Sulfates

Huxtable, Ryan J.

doi:10.1007/978-1-4757-9438-0_7

Cited by 3 publications

(5 citation statements)

References 119 publications

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“…The transfer of a sulphonate group (SO" − $ ) from a donor to an acceptor molecule is a fundamental process in the biotransformation of a host of endogenous compounds, as well as drugs and xenobiotics [1]. In order for sulphonation to occur, however, inorganic sulphate must be activated to a high-energy form prior to being transferred to an acceptor molecule [2,3].…”

Section: Introductionmentioning

confidence: 99%

Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms

Fuda

Shimizu

Lee

et al. 2002

Biochemical Journal

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Sulphonation, a fundamental process essential for normal growth and development, requires the sulphonate donor molecule 3h-phosphoadenosine 5h-phosphosulphate (PAPS), which is produced from ATP and inorganic sulphate by the bifunctional enzyme PAPS synthase. In humans, two genes encode isoenzymes that are 77 % identical at the amino acid level, and alternative splicing creates two subtypes of PAPS synthase 2. The question as to whether distinctions in amino acid composition are reflected in differences in activity has been examined. The specific activity of the PAPS synthase 2 subtypes is 10-to 15-fold higher than that for PAPS synthase 1. The greater catalytic efficiency of the PAPS synthase 2 subtypes is demonstrated further by the 3-to 6-fold higher k cat \K m ratios for ATP and inorganic sulphate as compared with the ratios for PAPS synthase 1. In humans, PAPS synthase 1 is expressed ubiquitously, and is the dominant isoform in most tissues, whereas expression of the PAPS synthase 2

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Section: Introductionmentioning

confidence: 99%

Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms

Fuda

Shimizu

Lee

et al. 2002

Biochemical Journal

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“…With pK a s < 1.5, steroid sulfonates remain fully ionized at any pH encountered in a biological system (10). As a consequence of increasing steroid polarity, sulfonation enhances water solubility and modifies protein binding, thereby influencing transportability.…”

Section: A Generalmentioning

confidence: 99%

“…Moreover, the enzymes that sulfoconjugate other relatively small endogenous compounds, such as catecholamines, iodothyronines, vitamin D, bile acids, and ascorbate, as well as the enzymes that sulfoconjugate xenobiotics, are also present in the cell sap (8,9). This is in contrast to sulfotransferases that catalyze the sulfonation of sulfolipids, such as sphingolipids and galactoglycerolipids, and macromolecules, such as proteins, proteoglycans, and glycosaminoglycans, which are associated with cell membranes and the Golgi complex (10). The sulfoconjugation of steroids involves the transfer of a sulfonate radical (SO 3~) from an activated donor molecule to an hydroxyl acceptor site.…”

Section: Introductionmentioning

confidence: 99%

“…The sulfoconjugation of steroids involves the transfer of a sulfonate radical (SO 3~) from an activated donor molecule to an hydroxyl acceptor site. This process, termed sulfonation, is to be distinguished from sulfation, which involves the transfer of a sulfate group (SO 4 2~) (10). Therefore, the products of sulfonation should be referred to as sulfonates, while the products of sulfation are referred to as sulfates.…”

Section: Introductionmentioning

confidence: 99%

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Steroid Sulfotransferases

Strott¹

1996

Endocrine Reviews

164

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“…These reactions involve enzymes termed sulfotransferases that are normally found in the soluble fraction of tissue preparations (2). Sulfonation involves the transfer of a sulfonate (SOG3) group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS), the universal sulfonate donor in mammals, to an hydroxyl acceptor site (3). A putative nucleotide binding motif containing the sequence GXXGXXK, first noted in N-heparan sulfate sulfotransferase (4), has been found in a highly conserved C-terminal region of all steroid and phenol sulfotransferases for which primary structures are known (5).…”

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confidence: 99%

The 3'-terminal exon of the family of steroid and phenol sulfotransferase genes is spliced at the N-terminal glycine of the universally conserved GXXGXXK motif that forms the sulfonate donor binding site.

Chiba¹,

Komatsu²,

Lee³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The guinea pig estrogen sulfotransferase gene has been cloned and compared to three other cloned steroid and phenol sulfotransferase genes (human estrogen sulfotransferase, human phenol sulfotransferase, and guinea pig 3av-hydroxysteroid sulfotransferase). The four sulfotransferase genes demonstrate a common outstanding feature: the splice sites for their 3'-terminal exons are identically located.That is, the 3'-terminal exon splice sites involve a glycine that constitutes the N-terminal glycine of an invariably conserved GXXGXXK motif present in all steroid and phenol sulfotransferases for which primary structures are known. This consistency strongly suggests that all steroid and phenol sulfotransferase genes will be similarly spliced. The GXXGXXK motif forms the active binding site for the universal sulfonate donor 3'-phosphoadenosine 5'-phosphosulfate. Amino acid sequence alignment of 19 cloned steroid and phenol sulfotransferases starting with the GXXGXXK motif indicates that the 3'-terminal exon for each steroid and phenol sulfotransferase gene encodes a similarly sized C-terminal fragment of the protein. Interestingly, on further analysis of the alignment, three distinct amino acid sequence patterns emerge. The presence of the conserved functional GXXGXXK motif suggests that the protein domains encoded by steroid and phenol sulfotransferase 3'-terminal exons have evolved from a common ancestor. Furthermnore, it is hypothesized that during the course of evolution, the 3'-terminal exon further diverged into at least three sulfotransferase subdivisions: a phenol or aryl group, an estrogen or phenolic steroid group, and a neutral steroid group.

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Sulfates

Cited by 3 publications

References 119 publications

Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms

Characterization and expression of human bifunctional 3′-phosphoadenosine 5′-phosphosulphate synthase isoforms

Steroid Sulfotransferases

The 3'-terminal exon of the family of steroid and phenol sulfotransferase genes is spliced at the N-terminal glycine of the universally conserved GXXGXXK motif that forms the sulfonate donor binding site.

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