Arylsulphatase activity in liver and gastrointestinal tract of sheep

Collett, Raymond A.

doi:10.1042/bst0080343

Cited by 4 publications

(1 citation statement)

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“…Arylsulphatase activity also was found in the wall of the gastrointestinal tract of sheep (Collett, 1980), and therefore the enzyme could be carried into rennet obtained from this species. Some bacterial species have also been shown to possess arylsulphatase activity, including Enterobacter aerogenes (Harada & Spencer, 1964), Salmonella species (Whitehead, Morrison, & Young, 1952;Murooka & Harada, 1981), Pseudomonas aeruginosa (Harada, 1964) and Klebsiella aerogenes (Adachi, Murooka, & Harada, 1975).…”

Section: Introductionmentioning

confidence: 97%

Arylsulphatase activity in milk and rennet from different sources

Kilic¹,

Lindsay²

2006

International Dairy Journal

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Section: Introductionmentioning

confidence: 97%

Arylsulphatase activity in milk and rennet from different sources

Kilic¹,

Lindsay²

2006

International Dairy Journal

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Arylsulfatase

Schomburg¹,

Salzmann²

1991

Enzyme Handbook 3

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Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1

Korban

Bobrov

Maynskova

et al. 2017

Protein Engineering, Design and Selection

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Sulfatases are a family of enzymes (sulfuric ester hydrolases, EC 3.1.6.-) that catalyze the hydrolysis of a wide array of sulfate esters. To date, despite the discovery of many sulfatase genes and the accumulation of data on numerous sulfated molecules, the number of characterized enzymes that are key players in sulfur metabolism remains extremely limited. While mammalian sulfatases are well studied due to their involvement in a wide range of normal and pathological biological processes, lower eukaryotic sulfatases, especially fungal sulfatases, have not been thoroughly investigated at the biochemical and structural level. In this paper, we describe the molecular cloning of Fusarium proliferatum sulfatase (F.p.Sulf-6His), its recombinant expression in Pichia pastoris as a soluble and active cytosolic enzyme and its detailed characterization. Gel filtration and native electrophoretic experiments showed that this recombinant enzyme exists as a tetramer in solution. The enzyme is thermo-sensitive, with an optimal temperature of 25°C. The optimal pH value for the hydrolysis of sulfate esters and stability of the enzyme was 6.0. Despite the absence of the post-translational modification of cysteine into Cα-formylglycine, the recombinant F.p.Sulf-6His has remarkably stable catalytic activity against p-nitrophenol sulfate, with kcat = 0.28 s-1 and Km = 2.45 mM, which indicates potential use in the desulfating processes. The currently proposed enzymatic mechanisms of sulfate ester hydrolysis do not explain the appearance of catalytic activity for the unmodified enzyme. According to the available models, the unmodified enzyme is not able to perform multiple catalytic acts; therefore, the enzymatic mechanism of sulfate esters hydrolysis remains to be fully elucidated.

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Arylsulphatase activity in liver and gastrointestinal tract of sheep

Cited by 4 publications

References 0 publications

Arylsulphatase activity in milk and rennet from different sources

Arylsulphatase activity in milk and rennet from different sources

Arylsulfatase

Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1

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