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Sulfur-containing amino acid
Methionine (symbol Met or M) (/mɪˈθaɪəniːn/) is an essential amino acid in humans. Compared to other amino acids, methionine has particularly decisive
Methionine
Chemical compound found in all domains of life with largely unexplored effects
S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or Adonat, is a common cosubstrate involved in methyl group transfers
S-Adenosyl_methionine
Mammalian protein found in humans
Methionine synthase (MS, MeSe, MTR) is primarily responsible for the regeneration of methionine from homocysteine in most individuals. In humans it is
Methionine_synthase
Chemical compound
Oxidation of the sulfur of methionine results in methionine sulfoxide or methionine sulfone. The sulfur-containing amino acids methionine and cysteine are more
Methionine_sulfoxide
Chemical compound
N-Formylmethionine (fMet, HCO-Met, For-Met) is a derivative of the amino acid methionine in which a formyl group has been added to the amino group. It is specifically
N-Formylmethionine
Chemical compound
Methionine sulfoximine (MSO, also known as MetSox) is an irreversible glutamine synthetase inhibitor. It is the sulfoximine derivative of methionine with
Methionine_sulfoximine
Chemical compound
post-translationally, arising by the double oxidation of methionine via the intermediate methionine sulfoxide. The methionine sulfone residue is found in the enzyme catalase
Methionine_sulfone
Methionine transaminase (EC 2.6.1.88, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo-acid aminotransferase. It
Methionine_transaminase
The enzyme methionine decarboxylase (EC 4.1.1.57) catalyzes the chemical reaction L-methionine ⇌ {\displaystyle \rightleftharpoons } 3-methylthiopropyl
Methionine_decarboxylase
Chemical compound
methionine by the removal of its terminal Cε methyl group. Although the production of homocysteine is a normal part of the metabolism of methionine,
Homocysteine
Disorder of amino acid metabolism
of the metabolism of the amino acid methionine due to a deficiency of cystathionine beta synthase or methionine synthase. It is an inherited autosomal
Homocystinuria
Medical condition
Hypermethioninemia is an excess of the amino acid methionine, in the blood. This condition can occur when methionine is not broken down properly in the body. Hypermethioninemia
Hypermethioninemia
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids
Methionine_gamma-lyase
Index of enzymes associated with the same name
Methionine sulfoxide reductase may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide reductase Peptide methionine sulfoxide reductase This
Methionine sulfoxide reductase
Methionine_sulfoxide_reductase
Chemical compound
L-Photo-methionine is a photo-reactive amino acid derivative of L-methionine that was synthetically formed in 2005. Protein are long polymer chains of
L-Photo-methionine
Small domesticated carnivorous mammal
niacin from tryptophan; inability to synthesise cysteine, citrulline, and methionine; lacks glucokinase activity; and an intolerance to glutamic acid (which
Cat
a methionine racemase (EC 5.1.1.2) is an enzyme that catalyzes the chemical reaction L-methionine ⇌ {\displaystyle \rightleftharpoons } D-methionine Hence
Methionine_racemase
Chemical process in which a methyl (CH3) group is covalently attached to a molecule
N-methylhistidine, and two isomers of N-methylarginine. Methionine synthase regenerates methionine (Met) from homocysteine (Hcy). The overall reaction transforms
Methylation
Protein-coding gene in the species Homo sapiens
reductase for methionine synthase and restores its cofactor to an active state allowing it to sustain folate and methionine metabolosis. Methionine is an essential
MTRR_(gene)
Class of enzymes
In enzymology, a methionine–tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction ATP + L-methionine + tRNAMet ⇌ {\displaystyle
Methionine–tRNA_ligase
Amino acids required in diet since they can not be synthesized in body
amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine. Six other
Essential_amino_acid
Protein-coding gene in the species Homo sapiens
Mitochondrial peptide methionine sulfoxide reductase, also known as methionine sulfoxide reductase A, is an enzyme that in humans is encoded by the MSRA
Mitochondrial peptide methionine sulfoxide reductase
Mitochondrial_peptide_methionine_sulfoxide_reductase
Chemical compound
S-Methylmethionine (SMM) is a derivative of methionine with the chemical formula (CH3)2S+CH2CH2CH(NH3+)CO2−. This cation is a naturally-occurring intermediate
S-Methylmethionine
Index of enzymes associated with the same name
Peptide methionine sulfoxide reductase may refer to: Protein-methionine-S-oxide reductase Peptide-methionine (S)-S-oxide reductase This set index page
Peptide methionine sulfoxide reductase
Peptide_methionine_sulfoxide_reductase
Class of enzymes
Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the
Methionyl_aminopeptidase
Set of biochemical processes
of lysine, asparagine, methionine, threonine, and isoleucine. Aspartate can be converted into lysine, asparagine, methionine and threonine. Threonine
Amino_acid_synthesis
Methionine S-methyltransferase (EC 2.1.1.12) is an enzyme that catalyzes the chemical reaction L-methionine + SAM S-methyl-L-methioninate
Methionine S-methyltransferase
Methionine_S-methyltransferase
Proteinogenic amino acid
body under normal physiological conditions if a sufficient quantity of methionine is available through the transsulfuration pathway. The majority of l-cysteine
Cysteine
Class of enzymes
[Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine
(Methionine synthase) reductase
(Methionine_synthase)_reductase
Metabolic pathway involving the transfer of a thiol group
allows the conversion of this intermediate to methionine, through a methylation reaction carried out by methionine synthase. The reverse pathway is present
Transsulfuration_pathway
Chemical compound (BrCN)
modify biopolymers, fragment proteins and peptides (cuts the C-terminus of methionine), and synthesize other compounds. The compound is classified as a pseudohalogen
Cyanogen_bromide
Domesticated species of canid
cannot synthesize ten: arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Like cats, dogs require
Dog
Amino acid
with L being assigned to the structurally simpler leucine, and M to methionine. Two pathways have been identified in nature for the synthesis of lysine
Lysine
Methionine-glyoxylate transaminase (EC 2.6.1.73) is an enzyme that catalyzes the chemical reaction L-methionine + glyoxylic acid
Methionine—glyoxylate transaminase
Methionine—glyoxylate_transaminase
Chemical compound
tomato, earthy, vegetable, creamy, oily" that is a degradation product of methionine. It is a notable flavor in potato-based snacks, namely potato chips, one
Methional
Protein-coding gene in humans
Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene. Methionine aminopeptidase 2, a member of the dimetallohydrolase
METAP2
Enzyme found in humans
Methionine–tRNA ligase, cytoplasmic, also called methionyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the MARS1 gene (formally MARS)
Methionine–tRNA ligase, cytoplasmic
Methionine–tRNA_ligase,_cytoplasmic
In enzymology, a L-methionine (R)-S-oxide reductase (EC 1.8.4.14) is an enzyme that catalyzes the chemical reaction L-methionine + thioredoxin disulfide
L-methionine (R)-S-oxide reductase
L-methionine_(R)-S-oxide_reductase
by solvent evaporation; they belong to the triclinic space group P1. L-methionine L-methioninium hydrogen maleate also belongs to the amino acid family
Organic nonlinear optical materials
Organic_nonlinear_optical_materials
First codon of a messenger RNA translated by a ribosome
transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and archaea and N-formylmethionine (fMet) in bacteria, mitochondria
Start_codon
Chemical compound
species. In vivo, selenomethionine is randomly incorporated instead of methionine. Selenomethionine is readily oxidized. Selenomethionine's antioxidant
Selenomethionine
Chemical compound
10-methylenetetrahydrofolate (MTHF) and used to recycle homocysteine back to methionine by methionine synthase (MS). L-methylfolate is water-soluble and primarily excreted
Levomefolic_acid
Protein domain
as methionine adenosyltransferase (MAT), is an enzyme that creates S-adenosylmethionine (also known as AdoMet, SAM or SAMe) by reacting methionine (a
S-Adenosylmethionine synthetase
S-Adenosylmethionine_synthetase
Methionine-S-oxide reductase (EC 1.8.4.5, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine sulfoxide reductase,
Methionine-S-oxide_reductase
Class of enzymes
{\displaystyle \rightleftharpoons } tetrahydropteroyltri-L-glutamate + L-methionine Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate
5-Methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase
5-Methyltetrahydropteroyltriglutamate—homocysteine_S-methyltransferase
methyltransferase (EC 2.1.1.137, S-adenosyl-L-methionine:arsenic(III) methyltransferase, S-adenosyl-L-methionine:methylarsonite As-methyltransferase, methylarsonite
Arsenite_methyltransferase
Chemical compound
and a thioether. The compound is structurally related to the amino acid methionine by replacement of the amine with a hydroxy group. The compound is produced
2-Hydroxy-4-(methylthio)butyric acid
2-Hydroxy-4-(methylthio)butyric_acid
Diet with reduced sulfur content
classified as essential mineral (e.g. elemental sulfur), essential amino acid (methionine) and semi-essential amino acid (e.g. cysteine). Sulfur is an essential
Low-sulfur_diet
Enzyme
(EC 2.1.1.254, EryG) is an enzyme with systematic name S-adenosyl-L-methionine:erythromycin C 3''-O-methyltransferase. This enzyme catalyses two related
Erythromycin 3''-O-methyltransferase
Erythromycin_3''-O-methyltransferase
Class of enzymes
S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase. This enzyme catalyses the following chemical reaction S-adenosyl-L-methionine + pseudouridine1915
23S rRNA (pseudouridine1915-N3)-methyltransferase
23S_rRNA_(pseudouridine1915-N3)-methyltransferase
Chemical element with atomic number 16 (S)
compounds or metal sulfides. Amino acids (two proteinogenic: cysteine and methionine, and many other non-coded: cystine, taurine, etc.) and two vitamins (biotin
Sulfur
reaction between fluoride ion and the co-factor S-adenosyl-L-methionine (SAM) to generate L-methionine and 5'-fluoro-5'-deoxyadenosine, the first committed product
Fluorinase
Class of enzymes
Peptide-methionine (S)-S-oxide reductase (EC 1.8.4.11, MsrA, methionine sulphoxide reductase A, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide
Peptide-methionine (S)-S-oxide reductase
Peptide-methionine_(S)-S-oxide_reductase
Chemical compound
and thermospermine. It is produced by decarboxylation of S-adenosyl methionine. This reaction is catalyzed by S-adenosylmethionine decarboxylase. The
S-Adenosylmethioninamine
Mepron is the brand name for a time-released, rumen-protected DL-Methionine capsule for dairy cattle. It is a registered trademark of Evonik Industries
Mepron (rumen-protected methionine)
Mepron_(rumen-protected_methionine)
Class of enzymes
S-Adenosyl-L-methionine + 1,2,3,4-tetrahydroisoquinoline, S-Adenosyl-L-methionine + isoquinoline, S-Adenosyl-L-methionine + quinoline, S-Adenosyl-L-methionine +
Nicotinamide N-methyltransferase
Nicotinamide_N-methyltransferase
8-O-methylsterigmatocystin. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised
Sterigmatocystin 8-O-methyltransferase
Sterigmatocystin_8-O-methyltransferase
analog. L-Photo-leucine and L-photo-methionine are analogs of the naturally occurring L-leucine and L-methionine amino acids that are endogenously incorporated
Photo-reactive amino acid analog
Photo-reactive_amino_acid_analog
Index of articles associated with the same name
sulfur amino acids include: Proteinogenic amino acids Cysteine (Cys, C) Methionine (Met or M), an essential amino acid in humans Metabolic products: Cystine
Sulfur_amino_acid
Protein-coding gene in the species Homo sapiens
Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the MSRB1 gene. This gene encodes a selenoprotein, which contains a selenocysteine
MSRB1
Chemical compound
human diet. In plants isoleucine can be synthesized from threonine and methionine. In plants and bacteria, isoleucine is synthesized from a pyruvate employing
Isoleucine
Chemical data page
Standard temperature and pressure. Reliability of data general note. ^a 63-68-3 EINECS for L-Methionine ^a CID 876 from PubChem ^a CID 6137 from PubChem
Methionine_(data_page)
Class of vitamins
a neurotoxic dicarboxylic acid, causing neurological deterioration. Methionine synthase, coded by MTR gene, is a methyltransferase enzyme which uses
Vitamin_B12
Iron (II) disulfide mineral
Organic sulfide CH3SCH3 Methionine Heterocycles C2H4S C4H4S Thiamine Biotin Thia-crown ether Sulfonium S-Adenosyl methionine S-Methylmethionine
Pyrite
Breakdown product of creatine phosphate
in the kidney from the amino acids arginine and glycine) by S-adenosyl methionine. It is then transported in the blood to other organs, muscles, and the
Creatinine
Chemical compound
a building block to other chemical compounds, such as the amino acid methionine. Acrolein was first named and characterized as an aldehyde by the Swedish
Acrolein
Pentapeptide
been found, one containing leucine ("leu"), and the other containing methionine ("met"). Both are products of the proenkephalin gene: Met-enkephalin is
Enkephalin
Class of enzymes
S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction S-adenosyl-L-methionine + adenosine1067
23S rRNA (adenosine1067-2'-O)-methyltransferase
23S_rRNA_(adenosine1067-2'-O)-methyltransferase
Class of enzymes
converted to ayanin. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). This enzyme belongs
3,7-dimethylquercetin 4'-O-methyltransferase
3,7-dimethylquercetin_4'-O-methyltransferase
Biological process
antifolates. A number of other biologically-important substances, like methionine and nicotinate, have their own salvage pathways to recycle parts of the
Nucleotide_salvage
Class of enzymes
m4C-forming MTase; S-adenosyl-L-methionine:DNA-cytosine 4-N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:DNA-cytosine N4-methyltransferase
Site-specific DNA-methyltransferase (cytosine-N4-specific)
Site-specific_DNA-methyltransferase_(cytosine-N4-specific)
Class of enzymes
S-adenosyl-L-methionine:8-hydroxyfuranocoumarin 8-O-methyltransferase, xanthotoxol methyltransferase, xanthotoxol O-methyltransferase, S-adenosyl-L-methionine:xanthotoxol
8-hydroxyfuranocoumarin 8-O-methyltransferase
8-hydroxyfuranocoumarin_8-O-methyltransferase
Class of enzymes
N-methyltransferase is an enzyme that catalyzes the chemical reaction: S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline ⇌ {\displaystyle \rightleftharpoons
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline_N-methyltransferase
Organic compounds containing amine and carboxylic groups
canonical amino acids. A modified form of methionine (N-formylmethionine) is often incorporated in place of methionine as the initial amino acid of proteins
Amino_acid
dimethylglycine N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:glycine(or sarcosine or N,N-dimethylglycine) N-methyltransferase (sarcosine(or
Glycine/sarcosine/dimethylglycine N-methyltransferase
Glycine/sarcosine/dimethylglycine_N-methyltransferase
S-adenosyl-L-methionine:tRNA (cytidine32/guanosine34-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction S-adenosyl-L-methionine +
TRNA (cytidine32/guanosine34-2'-O)-methyltransferase
TRNA_(cytidine32/guanosine34-2'-O)-methyltransferase
transferase, S-adenosyl-L-methionine:halide/bisulfide methyltransferase, AtHOL1, AtHOL2, AtHOL3, HMT, S-adenosyl-L-methionine: halide ion methyltransferase
Methyl_halide_transferase
Topics referred to by the same term
L-methionine:oxidized-thioredoxin S-oxidoreductase may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide reductase This disambiguation page
L-methionine:oxidized-thioredoxin S-oxidoreductase
L-methionine:oxidized-thioredoxin_S-oxidoreductase
In enzymology, a L-methionine (S)-S-oxide reductase (EC 1.8.4.13) is an enzyme that catalyzes the chemical reaction L-methionine + thioredoxin disulfide
L-methionine (S)-S-oxide reductase
L-methionine_(S)-S-oxide_reductase
homocysteine to the essential amino acid methionine. The remethylation process involves the enzyme methionine synthase (MS), which requires vitamin B12
Remethylation
Chemical compound
blood to the liver. A methyl group is added to GAA from the amino acid methionine by the enzyme GAMT, forming non-phosphorylated creatine. This is then
Phosphocreatine
Rate-limiting enzyme in the methyl cycle
toxic amino acid) to methionine by the enzyme methionine synthase. (Note that homocysteine can also be converted to methionine by the folate-independent
Methylenetetrahydrofolate reductase
Methylenetetrahydrofolate_reductase
Protein family
family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor. PLP is
Cys/Met metabolism PLP-dependent enzyme family
Cys/Met_metabolism_PLP-dependent_enzyme_family
Class of enzymes
converts S-adenosyl methionine to 5'-chloro-5'-deoxyadenosine and L-methionine using a chloride ion (Cl−): S-Adenosyl methionine Cl−
Adenosyl-chloride_synthase
Class of enzymes
produce dimethylglycine and methionine respectively: trimethylglycine + L-homocysteine dimethylglycine + L-methionine BHMT belongs to the family
Betaine—homocysteine S-methyltransferase
Betaine—homocysteine_S-methyltransferase
converted to fecosterol. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine
Sterol_24-C-methyltransferase
Form of vitamin B-12
4REQ) and methionine synthase (PDB 1Q8J). Methylcobalamin and 5-methyltetrahydrofolate are needed by methionine synthase in the methionine cycle to transfer
Cyanocobalamin
Class of enzymes
7-methylxanthosine. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised
7-methylxanthosine_synthase
Class of enzymes
converted to creatine. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine
Guanidinoacetate N-methyltransferase
Guanidinoacetate_N-methyltransferase
Group of chemical compounds
diphosphate-ethanolamine to diglycerides, releasing cytidine monophosphate. S-Adenosyl methionine can subsequently methylate the amine of phosphatidylethanolamines to yield
Phosphatidylethanolamine
Chemical compound
fluorinase catalyzed addition of a fluoride ion to S-adenosyl-L-methionine, releasing L-methionine as a by product. Purine nucleoside phosphorylase mediates
5'-Deoxy-5'-fluoroadenosine
Class of enzymes
1.1.243, mrsA (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase. This enzyme catalyses
2-Ketoarginine methyltransferase
2-Ketoarginine_methyltransferase
Chemical reactions forming cocaine
Biosynthesis of N-methyl-pyrrolinium cation. MeSR2+ refers to the methylating agent S-adenosyl methionine.
Biosynthesis_of_cocaine
Class of enzymes
S-adenosyl-L-methionine:27S pre-rRNA (guanosine2922-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction S-adenosyl-L-methionine + guanosine2922
27S pre-rRNA (guanosine2922-2'-O)-methyltransferase
27S_pre-rRNA_(guanosine2922-2'-O)-methyltransferase
Class of enzymes
S-adenosyl-L-methionine:23S rRNA (guanine2445-N2)-methyltransferase. This enzyme catalyses the following chemical reaction S-adenosyl-L-methionine + guanine2445
23S rRNA (guanine2445-N2)-methyltransferase
23S_rRNA_(guanine2445-N2)-methyltransferase
Enzyme
to ferulic acid. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme belongs
Caffeate_O-methyltransferase
Amino acid that is incorporated biosynthetically into proteins during translation
The essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine (i.e. H, I, L, K, M
Proteinogenic_amino_acid
Yellow legume seeds used as food
289 g Threonine 1.33 g Isoleucine 1.62 g Leucine 2.74 g Lysine 1.93 g Methionine 0.255 g Cystine 0.466 g Phenylalanine 1.44 g Tyrosine 1.36 g Valine 1
Lupin_bean
Free radical toxicity
needed] The amino acid methionine is prone to oxidation, but oxidation of methionine can be reversible. Oxidation of methionine is shown to inhibit the
Oxidative_stress
ROMT-15, HvOMT1, ZmOMT1) is an enzyme with systematic name S-adenosyl-L-methionine:tricetin 3',5'-O-dimethyltransferase. This enzyme catalyses the following
Tricin_synthase
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