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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.
Methionine, an essential sulfur containing amino acid. The recommended daily allowance (RDA) of methionine (combined with cysteine) for adults is set at 13–14 mg kg-1 day-1 (13–14 mg per kg of body weight per day), but some researchers have argued that this figure is too low, and should more appropriately be 25 mg kg-1 day-1. [1]
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.
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.
The sulfonium functional group present in S-adenosyl methionine is the center of its peculiar reactivity. Depending on the enzyme, S-adenosyl methionine can be converted into one of three products: adenosyl radical, which converts to deoxyadenosine (AdO): classic rSAM reaction, also cogenerates methionine
Glycyl-methionine or Gly-Met is a dipeptide consisting of the amino acids glycine and methionine. [1] It plays a role as a metabolite.
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.