Reactome: A Curated Pathway Database
All 10 results
Pathways (8) Reactions (1) Proteins (1) Others (0)
Protein: UniProt:P51690 ARSE (Homo sapiens)
Last changed: 2014-11-26 10:20:21

Pathway: Metabolism (Homo sapiens)
Metabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as the inactivation and elimination of toxic ones generated endogenously or present in the extracellular environment. The processes of energy metabolism can be classified into two groups according to whether the
Last changed: 2014-11-21 19:49:01

Pathway: Metabolism of proteins (Homo sapiens)
Protein metabolism comprises the pathways of translation, post-translational modification and protein folding
Last changed: 2014-11-21 19:49:01

Pathway: Sphingolipid metabolism (Homo sapiens)
Sphingolipids are derivatives of long chain sphingoid bases such as sphingosine (trans-1,3-dihydroxy 2-amino-4-octadecene), an 18-carbon unsaturated amino alcohol which is the most abundant sphingoid base in mammals. Amide linkage of a fatty acid to sphingosine yields ceramides. Esterification of phosphocholine to ceramides yields sphingomyelin, and ceramide glycosylation yields glycosylceramides. Intr
Last changed: 2014-11-21 19:49:01

Pathway: Post-translational protein modification (Homo sapiens)
After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the internal peptide bond cleavages that activate proenzymes, the attachment of oligosaccharide moieties to membrane-bound and secreted proteins, the attachment of lipid o
Last changed: 2014-11-21 19:49:01

Pathway: Metabolism of lipids and lipoproteins (Homo sapiens)
Lipids are hydrophobic but otherwise chemically diverse molecules that play a wide variety of roles in human biology. They include ketone bodies, fatty acids, triacylglycerols, phospholipids and sphingolipids, eicosanoids, cholesterol, bile salts, steroid hormones, and fat-soluble vitamins. They function as a major source of energy (fatty acids, triacylglycerols, and ketone bodies), are major constitue
Last changed: 2014-11-21 19:49:01

Pathway: Gamma carboxylation, hypusine formation and arylsulfatase activation (Homo sapiens)
After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the vitamin K-dependent attachment of carboxyl groups to glutamate residues and the conversion of a lysine residue in eIF5A to hypusine, and the conversion of a histidine
Last changed: 2014-11-21 19:49:01

Pathway: The activation of arylsulfatases (Homo sapiens)
Sulfatase activity requires a unique posttranslational modification (PTM) of a catalytic cysteine residue into a formylglycine. This modification is impaired in patients with multiple sulfatase deficiency (MSD) due to defects in the SUMF1 (sulfatase-modifying factor 1) gene responsible for this PTM. SUMF2 can inhibit the activity of SUMF1 thereby providing a mechanism for the regulation of sulfatase ac
Last changed: 2014-11-21 14:40:22

Pathway: Glycosphingolipid metabolism (Homo sapiens)
The steps involved in the synthesis of glycosphingolipids (sphingolipids with one or more sugars attached) are annotated here (Gault et al. 2010)
Last changed: 2014-11-21 19:49:01

Reaction: SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases (Homo sapiens)
The sulfatase-modifying factor 1 (SUMF1, also called C-alpha-formylglycine-generating enzyme, FGE) (Preusser-Kunze et al. 2005, Cosma et al. 2003, Landgrebe et al. 2003) oxidises the critical cysteine residue in arylsulfatases to an active site 3-oxoalanine residue thus confering sulfatase activity (Roeser et al. 2006). Defects in SUMF1 cause multiple sulfatase deficiency (MSD) (MIM:272200), an impairm
Last changed: 2014-11-21 14:40:22