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FMO3 is the main flavin-containing monooxygenase isoenzyme that is expressed in the liver of adult humans. [ 8 ] [ 9 ] [ 10 ] The human FMO3 enzyme catalyzes several types of reactions, including: the N -oxygenation of primary, secondary, and tertiary amines ; [ 9 ] [ 11 ] the S -oxygenation of nucleophilic sulfur -containing compounds; [ 9 ...
From the sulfide they form the amino acids cysteine and methionine, sulfolipids, and other sulfur compounds. Animals obtain sulfur from cysteine and methionine in the protein that they consume. Sulfur is the third most abundant mineral element in the body. [21] The amino acids cysteine and methionine are used by the body to make glutathione.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases. [1] This enzyme participates in cysteine metabolism. It is encoded by the MPST gene. [2] The enzyme is of interest because it provides a pathway for detoxification of cyanide, especially since it occurs widely in the cytosol and distributed broadly. [3]
The fractionations of oxygen produced by sulfur disproportionation from elemental sulfur have been found to be higher, with reported values from 8 to 18.4‰, which suggests a kinetic isotope effect in the pathways involved in oxidation of elemental sulfur to sulfate, although more studies are necessary to determine what are the specific steps ...
In biochemistry, sulfotransferases (SULTs) are transferase enzymes that catalyze the transfer of a sulfo group (R−SO − 3) from a donor molecule to an acceptor alcohol (R−OH) or amine (R−NH 2). [1] The most common sulfo group donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS).
Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN −) by converting it to thiocyanate (SCN −, also known as "rhodanate"). [1] In enzymatology, the common name is listed as thiosulfate sulfurtransferase (EC 2.8.1.1). [2] The diagram on the right shows the crystallographically-determined structure of rhodanese.
Mammalian SCL forms a homodimer while bacterial SCL is monomeric. In mammals, highest SCL activity is found in the liver and kidney. [1] [2]While selenocysteine lyases generally catalyze the removal of both selenium or sulfur from selenocysteine or cysteine, respectively, human selenocysteine lyases are specific for selenocysteine.
iduronate 2-sulfatase EC 3.1.6.13 (IDS), a lysosomal enzyme that hydrolyzes the 2-sulfate groups from iduronic acids in dermatan sulfate and heparan sulfate; N-acetylgalactosamine-6-sulfatase EC 3.1.6.4 , which hydrolyzes the 6-sulfate groups of the N-acetyl-D-galactosamine of chondroitin sulfate and D-galactose 6-sulfate units of keratan sulfate ;