SUMF1 explained

Sulfatase-modifying factor 1 is an enzyme that in humans is encoded by the SUMF1 gene.^{[1] [2] [3]}

Sulfatases catalyze the hydrolysis of sulfate esters such as glycosaminoglycans, sulfolipids, and steroid sulfates. C-alpha-formylglycine (FGly), the catalytic residue in the active site of eukaryotic sulfatases, is posttranslationally generated from a cysteine by SUMF1, the human form of the aerobic Formylglycine-generating enzyme (FGE), in the endoplasmic reticulum (ER). The genetic defect of FGly formation caused by mutations in the SUMF1 gene results in inactive FGE, and subsequently multiple sulfatase deficiency (MSD; MIM 272200), a lysosomal storage disorder (Roeser et al., 2006).[supplied by OMIM]

Further reading

• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–16903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Clark HF, Gurney AL, Abaya E, etal . The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment . Genome Res. . 13 . 10 . 2265–2270 . 2003 . 12975309 . 10.1101/gr.1293003 . 403697 .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–45 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Cosma MP, Pepe S, Parenti G, etal . Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency . Hum. Mutat. . 23 . 6 . 576–581 . 2004 . 15146462 . 10.1002/humu.20040 . 44637380 .
• Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–2127 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Preusser-Kunze A, Mariappan M, Schmidt B, etal . Molecular characterization of the human Calpha-formylglycine-generating enzyme . J. Biol. Chem. . 280 . 15 . 14900–14910 . 2005 . 15657036 . 10.1074/jbc.M413383200 . free .
• Dierks T, Dickmanns A, Preusser-Kunze A, etal . Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme . Cell . 121 . 4 . 541–552 . 2005 . 15907468 . 10.1016/j.cell.2005.03.001 . 2956795 . free .
• Otsuki T, Ota T, Nishikawa T, etal . Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries . DNA Res. . 12 . 2 . 117–126 . 2007 . 16303743 . 10.1093/dnares/12.2.117 . free .
• Roeser D, Preusser-Kunze A, Schmidt B, etal . A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme . Proc. Natl. Acad. Sci. U.S.A. . 103 . 1 . 81–86 . 2006 . 16368756 . 10.1073/pnas.0507592102 . 1324989 . 2006PNAS..103...81R . free .
• Fraldi A, Biffi A, Lombardi A, etal . SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies . Biochem. J. . 403 . 2 . 305–312 . 2007 . 17206939 . 10.1042/BJ20061783 . 1874239 .
• Annunziata I, Bouchè V, Lombardi A, etal . Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene . Hum. Mutat. . 28 . 9 . 928 . 2007 . 17657823 . 10.1002/humu.9504 . 8500605 . free .

Notes and References

1. Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K . Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme . Cell . 113 . 4 . 435–444 . May 2003 . 12757705 . 10.1016/S0092-8674(03)00347-7 . 11571659 . free .
2. Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A . The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases . Cell . 113 . 4 . 445–456 . May 2003 . 12757706 . 10.1016/S0092-8674(03)00348-9 . 15095377 . free .
3. Web site: Entrez Gene: SUMF1 sulfatase modifying factor 1.