| 词条 | Formylglycine-generating enzyme |
| 释义 |
| Name = Formylglycine-generating enzyme | EC_number =1.8.99 | CAS_number= | IUBMB_EC_number = | GO_code = | image = | width = | caption = }}{{Infobox protein family | Symbol = FGE-sulfatase | Name = Formylglycine-generating enzyme | image = PDB 2aik EBI.jpg | width = | caption = formylglycine generating enzyme c336s mutant covalently bound to substrate peptide lctpsra | Pfam = PF03781 | Pfam_clan = | InterPro = IPR005532 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}Formylglycine-generating enzyme (FGE) is the name for an enzyme that catalyzes the conversion of cysteine to formylglycine (fGly). There are two main classes of FGE, aerobic and anaerobic. FGE activates sulfatases, which are essential for the degradation of sulfate esters. The catalytic activity of sulfatases is dependent upon a formylglycine (sometimes called oxoalanine) residue in the active site.[1] AerobicThe aerobic enzyme has a structure homologous to the complex alpha/beta topology found in the gene product of human sulfatase-modifying factor 1 (SUMF1). Aerobic FGE converts a cysteine residue in the highly conserved consensus sequence CXPXR to fGly. AnaerobicThe most well-studied anaerobic FGE is the bacterial AtsB, an iron-sulfur cluster containing enzyme that is able to convert either cysteine or serine to fGly with a distinctly different mechanism than the aerobic form. Protein domainIn molecular biology, "formylglycine-generating enzyme" (sometimes annotated as formylglycine-generating sulfatase enzyme) is the name of the FGE protein domain, whether or not the protein is catalytically active. Disease statesIn humans, mutations in SUMF1 result in defects in FGE, which in turn causes the impairment of sulfatases. The result is a disease called multiple sulfatase deficiency (MSD), in which the accumulation of glycosaminoglycans or sulfolipids can cause early infant death.[2][3][4] Known substrates for SUMF1 are: N-acetylgalactosamine-6-sulfate sulfatase (GALNS), arylsulfatase A (ARSA), steroid sulfatase (STS) and arylsulfatase E (ARSE). SUMF1 occurs in the endoplasmic reticulum or its lumen. References1. ^{{cite journal |vauthors=Roeser D, Dickmanns A, Gasow K, Rudolph MG | title = De novo calcium/sulfur SAD phasing of the human formylglycine-generating enzyme using in-house data | journal = Acta Crystallogr. D | volume = 61 | issue = Pt 8 | pages = 1057–66 |date=August 2005 | pmid = 16041070 | doi = 10.1107/S0907444905013831 | url = }} {{InterPro content|IPR005532}}2. ^{{cite journal |vauthors=Fraldi A, Biffi A, Lombardi A, Visigalli I, Pepe S, Settembre C, Nusco E, Auricchio A, Naldini L, Ballabio A, Cosma MP | title = SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies | journal = Biochem. J. | volume = 403 | issue = 2 | pages = 305–12 |date=April 2007 | pmid = 17206939 | pmc = 1874239 | doi = 10.1042/BJ20061783 | url = }} 3. ^{{cite journal |vauthors=Diez-Roux G, Ballabio A | title = Sulfatases and human disease | journal = Annu Rev Genom Hum Genet | volume = 6 | issue = | pages = 355–79 | year = 2005 | pmid = 16124866 | doi = 10.1146/annurev.genom.6.080604.162334 | url = }} 4. ^{{cite journal |vauthors=Sardiello M, Annunziata I, Roma G, Ballabio A | title = Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship | journal = Hum. Mol. Genet. | volume = 14 | issue = 21 | pages = 3203–17 |date=November 2005 | pmid = 16174644 | doi = 10.1093/hmg/ddi351 | url = }} 1 : Protein domains |
| 随便看 |
|
开放百科全书收录14589846条英语、德语、日语等多语种百科知识，基本涵盖了大多数领域的百科知识，是一部内容自由、开放的电子版国际百科全书。