Arylsulfatase K, a Novel Lysosomal Sulfatase

Wiegmann, Elena Marie; Westendorf, Eva; Kalus, Ina; Pringle, Thomas H.; Lübke, Torben; Dierks, Thomas

doi:10.1074/jbc.m113.499541

Cited by 43 publications

(51 citation statements)

References 38 publications

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“…Two of these sulfatases, arylsulfatase K and ARSG, have been described and characterized only recently after heterologous ectopic expression (2,3). In this study, detailed biochemical description of the endogenous ARSG enzyme is presented to understand in vivo expression, function, and properties of this enzyme, which is critical for the degradation of 3-O-sulfated glucosamine residues of heparan sulfate.…”

Section: Discussionmentioning

confidence: 99%

“…3 By means of bioinformatics, 17 and 14 sulfatases have been identified in the human and murine genome, respectively, of which 13 have been characterized biochemically (1)(2)(3). Eight of these sulfatases are localized in lysosomes, where at least six of them are involved in the degradation of the GAGs heparan sulfate, dermatan sulfate, chondroitin sulfate, and keratan sulfate (4).…”

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confidence: 99%

“…Eight of these sulfatases are localized in lysosomes, where at least six of them are involved in the degradation of the GAGs heparan sulfate, dermatan sulfate, chondroitin sulfate, and keratan sulfate (4). The natural substrate of the very recently described lysosomal arylsulfatase K is yet unknown (2). Arylsulfatase A catalyzes the desulfation of the sulfolipid cerebroside 3-sulfate (5).…”

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confidence: 99%

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Molecular Characterization of Arylsulfatase G

Kowalewski

Lübke

Kollmann

et al. 2014

Journal of Biological Chemistry

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Background: Lysosomal arylsulfatase G (ARSG) is critical in heparan sulfate degradation. Results: ARSG is differentially expressed, processed, and transported in tissues involving a membrane-associated pre-lysosomal precursor; processing is dispensable for enzymatic activity. Conclusion: Although its lysosomal function is established, ARSG maturation and lysosomal targeting involve nontypical steps. Significance: These characteristics of ARSG need consideration when screening for ARSG-deficient mucopolysaccharidosis patients.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Molecular Characterization of Arylsulfatase G

Kowalewski

Lübke

Kollmann

et al. 2014

Journal of Biological Chemistry

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“…The gene encoding arylsulfatase K (ARSK; EC 3.1.6.13) (ARSK in vertebrates; Arsk in rodents) was initially identified using bioinformatic methods through its conserved sulfatase active site signature sequence [1,6] and subsequently cloned, expressed in human cells, purified and biochemically characterized as an arylsulfatase [7], recently identified as catalysing the hydrolysis of the 2-O-sulfate group from 2-sulfoglucuronate [8]. Kinetic properties for human ARSK were similar to those of several other lysosomal sulfatases and an established role in the degradation of sulfated glycosaminoglycans has been identified [8].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, low sequence identities with other human sulfatases have been reported, indicating that this gene and enzyme represents a distinct form of human sulfatase. Broad ARSK mRNA expression in human tissues has been reported which suggested that a ubiquitous biological arylsulfate substrate was the target for ARSK physiologically [7]. Previous studies have shown that it comprises several domains: an N-terminus signal peptide (residues ; five Ca 2+ binding sites (1 Ca 2+ per subunit); two active site residues (313Asp and 314His); and multiple N-glycosylation sites [7].…”

Section: Introductionmentioning

confidence: 99%

Vertebrate Arylsulfatase K (ARSK): Comparative and Evolutionary Studies of the Lysosomal 2-Sulfoglucuronate Sulfatase

Holmes¹

2018

J Data Mining Genomics Proteomics

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Arylsulfatase K (ARSK) is one of 17 sulfatase gene family members encoded on the human genome for which a role has been recently identified as a lysosomal 2-sulfoglucuronate sulfatase. Vertebrate ARSK sequences shared 60-82% identity but only <27% identities with other arylsulfatase family members. Comparative enzyme structures were studied, including residues with predicted roles in forming N-glycosylation sites, Ca 2+ binding and active site residues. Vertebrate ARSK genes usually contained 8 coding exons. A human ARSK gene promoter comprised CpG61 and multiple TFBS, which may be involved in signal transduction, transcription activation or regulating entry into cell division. Phylogenetic analyses examined evolutionary changes for the vertebrate ARSK and the invertebrate SUL1 genes. In summary, a major role for this enzyme as a 2-sulfoglucuronate sulfatase is supported which has been conserved throughout vertebrate evolution.Citation: Holmes RS (2017) Vertebrate Arylsulfatase K (ARSK): Comparative and Evolutionary Studies of the Lysosomal 2-Sulfoglucuronate Sulfatase.

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Enzymatic Kinetic Determinations

Hüttl

Frank

2000

Encyclopedia of Analytical Chemistry

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Kinetic methods for analytical applications can be divided into noncatalytic and catalytic methods. Enzyme kinetic determinations are a special type of catalytic methods. Enzymatic reactions are used analytically to determine enzyme activities – for instance, in the diagnosis of diseases, substrate concentrations in the food industry or medicine, and concentrations of effectors – for example, in trace analysis. Owing to the high selectivity of enzymatic analysis, the importance of this method in various fields is growing rapidly. The widest use is observed in clinical chemistry and food chemistry. This article gives only a general survey of the high potential of enzymatic analysis, with references to more detailed literature. Enzymatic reactions are characterized by some special features, explained after the introduction. The theoretical background for kinetic determination is the comprehension of the principles on enzymatic kinetics. In Section 3, the simplest mechanism, outlined by Michaelis and Menten, and several transformations of the equation are described. In this section, two kinetic parameters, enzyme activity and the Michaelis constant, are introduced. Section 4 deals with substances, the so‐called effectors , influencing the rate of an enzymatic reaction. Simple mechanisms of these effectors are shown. Different methods for determination of substrates, enzymes, and effectors, illustrated by many examples, are represented in Section 5. While substrate concentrations can be determined using both equilibrium or kinetic methods, the determination of enzymes and effectors can be performed only by kinetic approaches. In the last two sections, the application of enzymes in flow systems and biosensor development are shown.

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Arylsulfatase K, a Novel Lysosomal Sulfatase

Cited by 43 publications

References 38 publications

Molecular Characterization of Arylsulfatase G

Molecular Characterization of Arylsulfatase G

Vertebrate Arylsulfatase K (ARSK): Comparative and Evolutionary Studies of the Lysosomal 2-Sulfoglucuronate Sulfatase

Enzymatic Kinetic Determinations

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