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Methionine (symbol Met or M) [3] (/ m ɪ ˈ θ aɪ ə n iː n /) [4] is an essential amino acid in humans.. As the precursor of other non-essential amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans.
The 3 substrates of this enzyme are L-methionine, thioredoxin disulfide, and H 2 O, whereas its two products are L-methionine (R)-S-oxide and thioredoxin. This enzyme belongs to the family of oxidoreductases , specifically those acting on a sulfur group of donors with a disulfide as acceptor.
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes . Human proteins possessing this activity include METAP1 , METAP2 , METAP1D (mitochondrial), and RNPEPL1 .
During oxidative stress, methionine—tRNA ligase might be phosphorylated, which results in promiscuity of this enzyme, where it aminoacylates methionine to various non-Met tRNAs. This in turn leads to substitution of amino acids in proteins with methionine, which helps relieve oxidative stress in the cell.
In enzymology, a formylmethionine deformylase (EC 3.5.1.31) is an enzyme that catalyzes the chemical reaction. N-formyl-L-methionine + H 2 O formate + L-methionine. Thus, the two substrates of this enzyme are N-formyl-L-methionine and H 2 O, whereas its two products are formate and L-methionine.
Methionine sulfoximine (MSO, also known as MetSox [1]) is an irreversible glutamine synthetase inhibitor. It is the sulfoximine derivative of methionine with convulsant effects. [2] Methionine sulfoximine is composed of two different diastereomers, which are L-S-Methionine sulfoximine and L-R-Methionine sulfoximine.
Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S ...
In enzymology, a methionine gamma-lyase (EC 4.4.1.11) is an enzyme that catalyzes the chemical reaction. L-methionine + H 2 O methanethiol + NH 3 + 2-oxobutanoate. Thus, the two substrates of this enzyme are L-methionine and H 2 O, whereas its 3 products are methanethiol, NH 3, and 2-oxobutanoate.