Comparative and Evolutionary Studies of Vertebrate Extracellular Sulfatase Genes and Proteins: SULF1 and SULF2

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

“…Seven groups of these genes and proteins were identified, including ARS group 5 for a single human ARSK gene, which encodes a distinct 526 amino acid sequence enzyme and shares <27% sequence identities with other human arylsulfatases. This is in contrast to the sequence identities observed for other human enzyme ARS groups: Group 1 (ARSA, ARSG and GALNS) (33-39% identical); group 2 (ARSB, ARSI and ARSJ) (54-59%) [2]; group 3 (ARSD, ARSE, ARSF, ARSH and STS) (57-64%) [3]; and group 4 ARS sequences (SULF1, SULF2 and GNS) (42-67%) [5]. Groups 6 (SGSH) and 7 (IDS) [4] enzymes, however, exhibited distinct amino acid sequences which were 22% and 26% identical, respectively, with the human ARSK amino acid sequence ( Table 2).…”

“…Vertebrate ARSK genes and encoded proteins represent a distinct gene and protein arylsulfatase family which share key conserved sequences and domains reported for other arylsulfatase proteins previously studied [2][3][4][5][17][18][19][20]. The metabolic role for ARSK has recently been established and the natural substrate for this enzyme described as lysosomal 2-sulfoglucuronate, a key enzyme in the catabolism of heparin sulfate and dermatan sulfate [8].…”

“…ARSK and other human sulfatase genes and proteins: Proposed classification Table 2 summarises a classification scheme for 17 human sulfatase genes and proteins previously proposed, based on phylogenetic and amino acid sequence comparisons for human SULF1 and SULF2 (extracellular sulfatases 1 and 2) [5] and the other 15 human sulfatases, including the human ARSK gene and protein. Seven groups of these genes and proteins were identified, including ARS group 5 for a single human ARSK gene, which encodes a distinct 526 amino acid sequence enzyme and shares <27% sequence identities with other human arylsulfatases.…”

“…Seventeen human sulfatase gene families and fourteen mouse sulfatase gene families encode sulfatases which catalyse the hydrolysis of a range of biological sulfate esters in the body [1][2][3][4][5]. 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].…”

https://researchopenworld.com/heparan-sulfate-modifying-enzymes-intriguing-players-in-cancer-progression/#

“…In contrast, SULF2, but not SULF1, is a p53 target [31]. A comparison of potential transcription factor binding sites (TFBS) in the SULF1 and SULF2 promoter regions in silico revealed that ~50% of TBFS were not shared between these two genes [32]. Therefore, dysregulated transcriptional programs and different transcriptional targeting in SULF genes both in cancer cells and cells in the tumor microenvironment may partially explain some of the apparently contradicting data concerning SULF functions in tumorigenesis.…”