Record Information
Version2.0
Creation Date2012-05-31 13:00:34 -0600
Update Date2015-09-13 12:56:08 -0600
Secondary Accession Numbers
  • ECMDB00696
Identification
Name:L-Methionine
Description:L-Methionine, in addition to being a substrate for protein synthesis, is an intermediate in transmethylation reactions, serving as the major methyl group donor, including the methyl groups for DNA and RNA intermediates. Methionine is a methyl acceptor for 5-methyltetrahydrofolate-homocysteine methyl transferase (methionine synthase), the only reaction that allows for the recycling of this form of folate, and is also a methyl acceptor for the catabolism of betaine. Methionine is also required for synthesis of cysteine. Methionine is accepted as the metabolic precursor for cysteine. Only the sulfur atom from methionine is transferred to cysteine; the carbon skeleton of cysteine is donated by serine. (PMID 16702340)
Structure
Thumb
Synonyms:
  • (2S)-2-amino-4-(methylsulfanyl)butanoate
  • (2S)-2-amino-4-(methylsulfanyl)butanoic acid
  • (2S)-2-amino-4-(methylsulphanyl)butanoate
  • (2S)-2-amino-4-(methylsulphanyl)butanoic acid
  • (L)-methionine
  • (S)-(+)-methionine
  • (S)-2-amino-4-(methylthio)-Butanoate
  • (S)-2-amino-4-(methylthio)-Butanoic acid
  • (S)-2-Amino-4-(methylthio)butanoate
  • (S)-2-Amino-4-(methylthio)butanoic acid
  • (S)-2-amino-4-(methylthio)butyrate
  • (S)-2-amino-4-(methylthio)butyric acid
  • (S)-methionine
  • 2-Amino-4-(methylthio)butyrate
  • 2-Amino-4-(methylthio)butyric acid
  • 2-Amino-4-methylthiobutanoate
  • 2-Amino-4-methylthiobutanoic acid
  • a-amino-a-Aminobutyrate
  • a-amino-a-Aminobutyric acid
  • A-Amino-g-methylmercaptobutyrate
  • A-Amino-g-methylmercaptobutyric acid
  • Acimethin
  • Alpha-Amino-alpha-aminobutyrate
  • Alpha-Amino-alpha-aminobutyric acid
  • Alpha-Amino-gamma-methylmercaptobutyrate
  • Alpha-Amino-gamma-methylmercaptobutyric acid
  • Cymethion
  • G-Methylthio-a-aminobutyrate
  • G-Methylthio-a-aminobutyric acid
  • Gamma-Methylthio-alpha-aminobutyrate
  • Gamma-Methylthio-alpha-aminobutyric acid
  • H-Met-h
  • H-Met-oh
  • L(-)-amino-a-amino-a-Aminobutyrate
  • L(-)-amino-a-amino-a-Aminobutyric acid
  • L(-)-Amino-alpha-amino-alpha-aminobutyrate
  • L(-)-Amino-alpha-amino-alpha-aminobutyric acid
  • L(-)-amino-g-Methylthiobutyrate
  • L(-)-amino-g-Methylthiobutyric acid
  • L(-)-Amino-gamma-methylthiobutyrate
  • L(-)-Amino-gamma-methylthiobutyric acid
  • L(-)-amino-α-amino-α-Aminobutyrate
  • L(-)-amino-α-amino-α-Aminobutyric acid
  • L(-)-amino-γ-Methylthiobutyrate
  • L(-)-amino-γ-Methylthiobutyric acid
  • L-(-)-Methionine
  • L-2-Amino-4-(methylthio)butyrate
  • L-2-Amino-4-(methylthio)butyric acid
  • L-2-amino-4-Methylthiobutyrate
  • L-2-Amino-4-methylthiobutyric acid
  • L-2-Amino-4methylthiobutyrate
  • L-2-Amino-4methylthiobutyric acid
  • L-a-amino-g-Methylmercaptobutyrate
  • L-a-amino-g-Methylmercaptobutyric acid
  • L-a-Amino-g-methylthiobutyrate
  • L-a-Amino-g-methylthiobutyric acid
  • L-alpha-Amino-gamma-methylmercaptobutyrate
  • L-alpha-Amino-gamma-methylmercaptobutyric acid
  • L-alpha-Amino-gamma-methylthiobutyrate
  • L-alpha-Amino-gamma-methylthiobutyric acid
  • L-g-methylthio-a-Aminobutyrate
  • L-g-methylthio-a-Aminobutyric acid
  • L-gamma-Methylthio-alpha-aminobutyrate
  • L-gamma-Methylthio-alpha-aminobutyric acid
  • L-Methionin
  • L-Methionine
  • L-Methioninum
  • L-α-amino-γ-Methylmercaptobutyrate
  • L-α-amino-γ-Methylmercaptobutyric acid
  • L-α-amino-γ-Methylthiobutyrate
  • L-α-amino-γ-Methylthiobutyric acid
  • L-γ-methylthio-α-Aminobutyrate
  • L-γ-methylthio-α-Aminobutyric acid
  • Liquimeth
  • M
  • Mepron
  • MET
  • Methilanin
  • Methionine
  • Methioninum
  • Metionina
  • Neo-methidin
  • Poly-L-methionine
  • Polymethionine
  • S-Methionine
  • S-Methyl-L-homocysteine
  • Toxin WAR
  • α-amino-α-Aminobutyrate
  • α-amino-α-Aminobutyric acid
  • α-amino-γ-Methylmercaptobutyrate
  • α-amino-γ-Methylmercaptobutyric acid
  • γ-methylthio-α-Aminobutyrate
  • γ-methylthio-α-Aminobutyric acid
Chemical Formula:C5H11NO2S
Weight:Average: 149.211
Monoisotopic: 149.051049291
InChI Key:FFEARJCKVFRZRR-BYPYZUCNSA-N
InChI:InChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
CAS number:63-68-3
IUPAC Name:(2S)-2-amino-4-(methylsulfanyl)butanoic acid
Traditional IUPAC Name:L-methionine
SMILES:CSCC[C@H](N)C(O)=O
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as methionine and derivatives. These are compounds containing methionine or a derivative thereof resulting from reaction of methionine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomChemical entities
Super ClassOrganic compounds
ClassOrganic acids and derivatives
Sub ClassCarboxylic acids and derivatives
Direct ParentMethionine and derivatives
Alternative Parents
Substituents
  • Methionine or derivatives
  • Alpha-amino acid
  • L-alpha-amino acid
  • Thia fatty acid
  • Fatty acid
  • Fatty acyl
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Thioether
  • Sulfenyl compound
  • Dialkylthioether
  • Amine
  • Organic oxygen compound
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Organic nitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Organopnictogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:284 °C
Experimental Properties:
PropertyValueSource
Water Solubility:56.6 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 56.6 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogP:-1.87 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility23.9 mg/mLALOGPS
logP-1.9ALOGPS
logP-2.2ChemAxon
logS-0.8ALOGPS
pKa (Strongest Acidic)2.53ChemAxon
pKa (Strongest Basic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity37.59 m3·mol-1ChemAxon
Polarizability15.5 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Methionine sulfoxide + Reduced Thioredoxin > Water + L-Methionine + Oxidized Thioredoxin
Methionine sulfoxide + Reduced Thioredoxin > Water + L-Methionine + Oxidized Thioredoxin
Adenosine triphosphate + Water + L-Methionine > ADP + Hydrogen ion + L-Methionine + Phosphate
Adenosine triphosphate + Water + L-Methionine > ADP + Hydrogen ion + L-Methionine + Phosphate
5-Methyltetrahydrofolic acid + L-Homocysteine <> Hydrogen ion + L-Methionine + Tetrahydrofolic acid
L-Homocysteine + S-Methylmethionine > Hydrogen ion +2 L-Methionine
S-Adenosylmethionine + L-Homocysteine + S-Methylmethionine <> S-Adenosylhomocysteine + Hydrogen ion + L-Methionine
[4Fe-4S] iron-sulfur cluster + 2 S-Adenosylmethionine + Hydrogen ion + NAD + octanoate (protein bound) > [2Fe-2S] iron-sulfur cluster +2 5'-Deoxyadenosine +2 Iron + lipoate (protein bound) +2 L-Methionine + NADH
[2Fe-2S] iron-sulfur cluster + S-Adenosylmethionine + Dethiobiotin > [2Fe-1S] desulfurated iron-sulfur cluster + Biotin + 5'-Deoxyadenosine + Hydrogen ion + L-Methionine
Adenosine triphosphate + L-Methionine + tRNA(Met) > Adenosine monophosphate + L-Methionyl-tRNA (Met) + Pyrophosphate
Adenosine triphosphate + Water + L-Methionine <> S-Adenosylmethionine + Phosphate + Pyrophosphate
2 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IX
S-Adenosylmethionine + NADPH + L-Tyrosine > p-Cresol + 5'-Deoxyadenosine + Dehydroglycine + Hydrogen ion + L-Methionine + NADP
Hydrogen peroxide + L-Methionine > Water + Methionine sulfoxide
Hydrogen peroxide + L-Methionine > Water + Methionine sulfoxide
Phosphate + Pyrophosphate + S-Adenosylmethionine <> Adenosine triphosphate + L-Methionine + Water
S-Adenosylmethionine + L-Homocysteine <> S-Adenosylhomocysteine + L-Methionine
5-Methyltetrahydrofolic acid + L-Homocysteine <> Tetrahydrofolic acid + L-Methionine
Dethiobiotin + Sulfur donor + 2 S-Adenosylmethionine + 2 e- + 2 Hydrogen ion <> Biotin +2 L-Methionine +2 5'-Deoxyadenosine
4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <> 5-Aminoimidazole ribonucleotide + 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO
Adenosine triphosphate + L-Methionine + tRNA(Met) + tRNA(Met) <> Adenosine monophosphate + Pyrophosphate + L-Methionyl-tRNA + L-Methionyl-tRNA
5-Methyltetrahydropteroyltri-L-glutamic acid + L-Homocysteine <> Tetrahydropteroyltri-L-glutamic acid + L-Methionine
Coproporphyrin III + 2 S-Adenosylmethionine <> Protoporphyrinogen IX +2 Carbon dioxide +2 L-Methionine +2 5'-Deoxyadenosine
2-Oxo-4-methylthiobutanoic acid + L-Glutamate <> L-Methionine + alpha-Ketoglutarate
Protein N6-(octanoyl)lysine + 2 Sulfur donor + 2 S-Adenosylmethionine + Protein N6-(octanoyl)lysine <> Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine + Protein N6-(lipoyl)lysine
Octanoyl-[acp] + 2 Sulfur donor + 2 S-Adenosylmethionine <> Lipoyl-[acp] +2 L-Methionine +2 5'-Deoxyadenosine
L-Methionine + Hydrogen peroxide > L-methionine <i>S</i>-oxide + Water
Hydrogen ion + &alpha;-D-ribose-1-methylphosphonate-5-phosphate + S-Adenosylmethionine > &alpha;-D-ribose-1,2-cyclic-phosphate-5-phosphate + methane + 5'-Deoxyadenosine + L-Methionine
L-Methionine + Acetyl-CoA N-&alpha;-acetyl-L-methionine + Coenzyme A
<i>S</i>-sulfanyl-[acceptor] + Dethiobiotin + S-Adenosylmethionine > an unsulfurated sulfur acceptor + Biotin + 5'-Deoxyadenosine + L-Methionine + Hydrogen ion
a protein with N-terminal methionine + Water > L-Methionine + Peptides
Coproporphyrinogen III + S-Adenosylmethionine > Protoporphyrinogen IX + Carbon dioxide + L-Methionine + 5'-Deoxyadenosine
L-Homocysteine + 5-Methyltetrahydropteroyltri-L-glutamic acid > L-Methionine + tetrahydropteroyl tri-L-glutamate
L-Homocysteine + 5-Methyltetrahydrofolic acid L-Methionine + Tetrahydrofolic acid
L-Homocysteine + S-Adenosylmethionine Hydrogen ion + L-Methionine + S-Adenosylhomocysteine
S-methyl-L-methionine + L-Homocysteine Hydrogen ion + L-Methionine
5-Aminoimidazole ribonucleotide + S-Adenosylmethionine 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + carbon monoxide + Hydrogen ion
L-Methionine + a 2-oxo carboxylate 2-Oxo-4-methylthiobutanoic acid + a standard &alpha; amino acid
S-Adenosylmethionine + Ribonuc-tri-P-reductases-inactive <> 5'-Deoxyadenosine + L-Methionine + Ribonuc-tri-P-reductases-active
L-Tyrosine + S-Adenosylmethionine + a reduced electron acceptor > Dehydroglycine + p-Cresol + 5'-Deoxyadenosine + L-Methionine + an oxidized electron acceptor + Hydrogen ion
Water + Adenosine triphosphate + L-Methionine > Phosphate + ADP + L-Methionine + Hydrogen ion
Water + Adenosine triphosphate + L-Methionine > Phosphate + ADP + L-Methionine + Hydrogen ion
N-6-isopentyl adenosine-37 tRNA + S-Adenosylmethionine + <i>S</i>-sulfanyl-[acceptor] 2-methylthio-N-6-isopentyl adenosine-37 tRNA + S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + an unsulfurated sulfur acceptor + Hydrogen ion
6-Carboxy-5,6,7,8-tetrahydropterin + S-Adenosylmethionine + Hydrogen ion > 7-carboxy-7-deazaguanine + 5'-Deoxyadenosine + L-Methionine + Ammonia
gly-met + Water > Glycine + L-Methionine
methionine-alanine dipeptide + Water > L-Methionine + L-Alanine
Adenosine triphosphate + L-Methionine + Water > Phosphate + Pyrophosphate + S-Adenosylmethionine
Dethiobiotin + Hydrogen sulfide + 2 S-adenosyl-L-methionine > Biotin +2 L-Methionine +2 5'-Deoxyadenosine
Coproporphyrinogen III + 2 S-adenosyl-L-methionine > Protoporphyrinogen IX +2 Carbon dioxide +2 L-Methionine +2 5'-Deoxyadenosine
Protein N(6)-(octanoyl)lysine + 2 Hydrogen sulfide + 2 S-adenosyl-L-methionine > protein N(6)-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine
5-methyltetrahydropteroyltri-L-glutamate + L-Homocysteine > tetrahydropteroyltri-L-glutamate + L-Methionine
5-Methyltetrahydrofolic acid + L-Homocysteine > Tetrahydrofolic acid + L-Methionine
Adenosine triphosphate + L-Methionine + Water > Inorganic phosphate + Pyrophosphate + S-adenosyl-L-methionine
S-methyl-L-methionine + L-Homocysteine >2 L-Methionine
L-Methionine + thioredoxin disulfide + Water > L-methionine (S)-S-oxide + thioredoxin
L-Methionine + thioredoxin disulfide + Water > L-Methionine (R)-S-oxide + thioredoxin
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine > 5'-Deoxyadenosine + L-Methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine > 5'-Deoxyadenosine + L-Methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine > 5'-Deoxyadenosine + L-Methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
S-adenosyl-L-methionine + 7-Aminomethyl-7-deazaguanosine > L-Methionine + Adenine + epoxyqueuosine
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA > S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + 2-methyladenine(2503) in 23S rRNA
Adenosine triphosphate + L-Methionine + tRNA(Met) > Adenosine monophosphate + Pyrophosphate + L-methionyl-tRNA(Met)
5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine > 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO
L-Tyrosine + S-adenosyl-L-methionine + reduced acceptor > 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + acceptor +2 Hydrogen ion
L-Methionine + a 2-oxo acid > 2-Oxo-4-methylthiobutanoic acid + an L-amino acid
Acetyl-CoA + L-Methionine > CoA + N-Acetyl-L-methionine
2 S-Adenosylmethionine <> S-Adenosylhomocysteine +2 L-Methionine + 5'-Deoxyadenosine
2 S-Adenosylmethionine + Reduced acceptor <> S-Adenosylhomocysteine +2 L-Methionine + 5'-Deoxyadenosine
L-Tyrosine + S-Adenosylmethionine + NADPH <> 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ion
Peptide-L-methionine + Thioredoxin disulfide + Water + L-Methionine <> Peptide-L-methionine (S)-S-oxide + Thioredoxin + L-methionine (S)-S-oxide
Dethiobiotin + 2 S-adenosyl-L-methionine + 2 Hydrogen ion + a sulfurated [sulfur carrier] > Biotin +2 L-Methionine +2 5'-Deoxyadenosine
Octanoyl-[acyl-carrier protein] + 2 a sulfur donor + 2 S-adenosyl-L-methionine > Lipoyl-ACP +2 L-Methionine + 5'-Deoxyadenosine
Protein N6-(octanoyl)lysine + 2 a sulfur donor + 2 S-adenosyl-L-methionine > Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine
Protein N6-(octanoyl)lysine + 2 Reduced ferredoxin + 2 a sulfurated [sulfur carrier]  + 2 S-adenosyl-L-methionine >2 L-Methionine +2 5'-Deoxyadenosine + Oxidized ferredoxin + Protein N6-(lipoyl)lysine + an unsulfurated [sulfur carrier]
5-Methyltetrahydrofolic acid + Homocysteine + 5-Methyltetrahydrofolic acid + Homocysteine > Tetrahydrofolic acid + L-Methionine + Tetrahydrofolic acid
Homocysteine + N5-methyl--tetrahydropteroyl tri-L-glutamate + Homocysteine > L-Methionine + tetrahydropteroyltri-L-glutamate
L-Methionine + Adenosine triphosphate + Hydrogen ion + tRNA(Met) > Adenosine monophosphate + Pyrophosphate + L-methionyl-tRNA(Met)
Homocysteine + N5-methyl--tetrahydropteroyl tri-L-glutamate + Homocysteine > tetrahydropteroyltri-L-glutamate + L-Methionine
L-Methionine + Water + Adenosine triphosphate > Phosphate + Pyrophosphate
L-Methionine + Water + Adenosine triphosphate > Phosphate + Pyrophosphate + S-adenosyl-L-methionine
S-adenosyl-L-methionine + Coproporphyrinogen III > 5'-Deoxyadenosine + L-Methionine + Carbon dioxide + Protoporphyrinogen IX
L-Tyrosine + NADPH + S-adenosyl-L-methionine + L-Tyrosine + NADPH > Hydrogen ion + NADP + L-Methionine + 5'-Deoxyadenosine + p-Cresol + 2-iminoacetate
7-aminomethyl-7-deazaguanosine34 in tRNA + S-adenosyl-L-methionine > Hydrogen ion + L-Methionine + Adenine + epoxyqueuosine
L-Methionine + Adenosine triphosphate + Water > Adenosine diphosphate + Phosphate + Hydrogen ion + L-Methionine + ADP
L-Methionine + Adenosine triphosphate + Water > Adenosine diphosphate + Phosphate + Hydrogen ion + L-Methionine + ADP
L-Methionine + Adenosine triphosphate + Water > Adenosine diphosphate + Pyrophosphate + Hydrogen ion + L-Methionine + ADP
L-Methionine + Adenosine triphosphate + Water > Adenosine diphosphate + Pyrophosphate + Hydrogen ion + L-Methionine + ADP
Homocysteine + S-Methylmethionine <>2 L-Methionine + Hydrogen ion
5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine >3 Hydrogen ion + CO + Formic acid + L-Methionine + 5'-Deoxyadenosine + 4-amino-2-methyl-5-phosphomethylpyrimidine
L-Tyrosine + S-adenosyl-L-methionine + NADPH > Dehydroglycine + 4-Methylcatechol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ion
a [lipoyl-carrier protein] N6-octanoyl-L-lysine + 2 S-adenosyl-L-methionine + 2 a sulfurated [sulfur carrier]  + 2 Reduced ferredoxin > Protein N6-(lipoyl)lysine +2 5'-Deoxyadenosine +2 L-Methionine +2 an unsulfurated [sulfur carrier] +2 Oxidized ferredoxin
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SMPDB Pathways:
Biotin metabolismPW000762 Pw000762Pw000762 greyscalePw000762 simple
Lipoate Biosynthesis and Incorporation IPW002107 Pw002107Pw002107 greyscalePw002107 simple
Lipoic acid metabolismPW000770 Pw000770Pw000770 greyscalePw000770 simple
One Carbon Pool by Folate IPW001735 Pw001735Pw001735 greyscalePw001735 simple
One carbon pool by folatePW000773 Pw000773Pw000773 greyscalePw000773 simple
Porphyrin metabolismPW000936 Pw000936Pw000936 greyscalePw000936 simple
S-adenosyl-L-methionine biosynthesisPW000837 Pw000837Pw000837 greyscalePw000837 simple
S-adenosyl-L-methionine cyclePW002080 Pw002080Pw002080 greyscalePw002080 simple
Thiamin diphosphate biosynthesisPW002028 Pw002028Pw002028 greyscalePw002028 simple
Thiazole Biosynthesis IPW002041 Pw002041Pw002041 greyscalePw002041 simple
methionine biosynthesisPW000814 Pw000814Pw000814 greyscalePw000814 simple
preQ0 metabolismPW001893 Pw001893Pw001893 greyscalePw001893 simple
tRNA Charging 2PW000803 Pw000803Pw000803 greyscalePw000803 simple
tRNA chargingPW000799 Pw000799Pw000799 greyscalePw000799 simple
tyrosine biosynthesisPW000806 Pw000806Pw000806 greyscalePw000806 simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
145± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
129± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
66± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
30± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
58± 7 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
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43± 5 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
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Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-004i-0920000000-945c85aa7c9f5eb2dfbbView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-004i-0910000000-b837ee0f4413856560f1View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-00b9-7910000000-5a1558fbb2f5e86edc9bView in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-0udi-1900000000-1a97567ce4f25c4e8263View in MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-004i-0910000000-1b0477118cb20549bf4dView in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-0mbd-9200000000-77e5cfb78936ad02d71cView in MoNA
GC-MSGC-MS Spectrum - EI-Bsplash10-004i-0920000000-8ffae5d87508e0704903View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOFsplash10-004i-0920000000-945c85aa7c9f5eb2dfbbView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOFsplash10-004i-0910000000-b837ee0f4413856560f1View in MoNA
GC-MSGC-MS Spectrum - GC-EI-QQsplash10-01bc-2692000000-c6a4af434abaeea2de87View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOFsplash10-00b9-7910000000-5a1558fbb2f5e86edc9bView in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-0udi-1900000000-1a97567ce4f25c4e8263View in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-004i-0910000000-1b0477118cb20549bf4dView in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-00di-9510000000-c03dec8575710eed861eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-0uea-1900000000-b991859b2c5bed6592a8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-08fr-9000000000-66855ace60e59837f131View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-08fr-9000000000-56a567791c824c6a9da6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0fe0-0900000000-d680295f21b2e2b40366View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-9000000000-062d3540db4db22da836View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-0900000000-84467513e2c9ec1a6851View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-001i-0900000000-88dc2bebb198eea550efView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udi-0920000000-b444ad79abeb16acde43View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-001i-0900000000-6e24a8df417e5f3db58cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-0900000000-c60ef880eb9a816a274bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-000i-0900000000-a7b7d1a3481c0c691a5bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-0002-0900000000-9156f088f4cc9eafa892View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-0002-9200000000-f78ba2aab8d5a0e0b135View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-0002-9000000000-e7b819fd2d0ac3862860View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Negativesplash10-0002-9000000000-b61396e720381bd5ff85View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Negativesplash10-0002-9000000000-b61396e720381bd5ff85View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Positivesplash10-0udi-0900000000-c3557cb41fd6fe268819View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Positivesplash10-0udi-6900000000-6bf5af2d1c561013948aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Positivesplash10-08fr-9000000000-63c9b1c138f9a27490e5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Positivesplash10-03di-9000000000-e133c47b0efe4992589fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Positivesplash10-03di-9000000000-dee78b4f34f8732fedb0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - CE-ESI-TOF (CE-system connected to 6210 Time-of-Flight MS, Agilent) , Positivesplash10-0udi-0900000000-d3f03ff5e8eacc8b6c8eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Positivesplash10-0udi-0900000000-e0dd5ff44b7962f6a2d2View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0udi-2900000000-305916dde72c899993b6View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udi-9800000000-47e0a34a2ec02bd762bfView in MoNA
1D NMR13C NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Alme B, Bremmelgaard A, Sjovall J, Thomassen P: Analysis of metabolic profiles of bile acids in urine using a lipophilic anion exchanger and computerized gas-liquid chromatorgaphy-mass spectrometry. J Lipid Res. 1977 May;18(3):339-62. Pubmed: 864325
  • Alton KB, Hernandez A, Alvarez N, Patrick JE: High-performance liquid chromatographic determination of N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methionine, the active plasma metabolite of a prodrug atriopeptidase inhibitor (SCH 42495), using a thiol selective (Au/Hg) amperometric detector. J Chromatogr. 1992 Sep 2;579(2):307-17. Pubmed: 1429978
  • Ball, R. O., Courtney-Martin, G., Pencharz, P. B. (2006). "The in vivo sparing of methionine by cysteine in sulfur amino acid requirements in animal models and adult humans." J Nutr 136:1682S-1693S. Pubmed: 16702340
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216
  • Ditscheid B, Funfstuck R, Busch M, Schubert R, Gerth J, Jahreis G: Effect of L-methionine supplementation on plasma homocysteine and other free amino acids: a placebo-controlled double-blind cross-over study. Eur J Clin Nutr. 2005 Jun;59(6):768-75. Pubmed: 15870821
  • Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. Pubmed: 12834252
  • Fischer JL, Lancia JK, Mathur A, Smith ML: Selenium protection from DNA damage involves a Ref1/p53/Brca1 protein complex. Anticancer Res. 2006 Mar-Apr;26(2A):899-904. Pubmed: 16619485
  • Garlick PJ: Toxicity of methionine in humans. J Nutr. 2006 Jun;136(6 Suppl):1722S-1725S. Pubmed: 16702346
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. Pubmed: 6198473
  • Harth G, Horwitz MA: Inhibition of Mycobacterium tuberculosis glutamine synthetase as a novel antibiotic strategy against tuberculosis: demonstration of efficacy in vivo. Infect Immun. 2003 Jan;71(1):456-64. Pubmed: 12496196
  • Hesse A, Heimbach D: Causes of phosphate stone formation and the importance of metaphylaxis by urinary acidification: a review. World J Urol. 1999 Oct;17(5):308-15. Pubmed: 10552150
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Kersemans V, Cornelissen B, Kersemans K, Bauwens M, Achten E, Dierckx RA, Mertens J, Slegers G: In vivo characterization of 123/125I-2-iodo-L-phenylalanine in an R1M rhabdomyosarcoma athymic mouse model as a potential tumor tracer for SPECT. J Nucl Med. 2005 Mar;46(3):532-9. Pubmed: 15750170
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
  • Sardharwalla IB, Fowler B, Robins AJ, Komrower GM: Detection of heterozygotes for homocystinuria. Study of sulphur-containing amino acids in plasma and urine after L-methionine loading. Arch Dis Child. 1974 Jul;49(7):553-9. Pubmed: 4851308
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. Pubmed: 2026685
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  • Takasu A, Shimosegawa T, Shimosegawa E, Hatazawa J, Kimura K, Fujita M, Koizumi M, Kanno I, Toyota T: 11C-methionine uptake to the pancreas and its secretion: a positron emission tomography study in humans. Pancreas. 1999 May;18(4):392-8. Pubmed: 10231845
  • van de Poll MC, Dejong CH, Soeters PB: Adequate range for sulfur-containing amino acids and biomarkers for their excess: lessons from enteral and parenteral nutrition. J Nutr. 2006 Jun;136(6 Suppl):1694S-1700S. Pubmed: 16702341
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. Pubmed: 18402659
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Boy, Matthias; Klein, Daniela; Schroeder, Hartwig. Method for the production and recovery of methionine. PCT Int. Appl. (2005), 34 pp.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID16811
HMDB IDHMDB00696
Pubchem Compound ID6137
Kegg IDC00073
ChemSpider ID5907
WikipediaMET
BioCyc IDMET
EcoCyc IDMET
Ligand ExpoMET_LFZW

Enzymes

General function:
Involved in nucleotide binding
Specific function:
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
Gene Name:
metG
Uniprot ID:
P00959
Molecular weight:
76254
Reactions
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).
General function:
Involved in transferase activity
Specific function:
An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate
Gene Name:
tyrB
Uniprot ID:
P04693
Molecular weight:
43537
Reactions
An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.
General function:
Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Specific function:
Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Gene Name:
msrA
Uniprot ID:
P0A744
Molecular weight:
23315
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.
General function:
Involved in peptide-methionine-(S)-S-oxide reductase activity
Specific function:
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin
Gene Name:
msrB
Uniprot ID:
P0A746
Molecular weight:
15451
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth
Gene Name:
metK
Uniprot ID:
P0A817
Molecular weight:
41951
Reactions
ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in catalytic activity
Specific function:
Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflA
Uniprot ID:
P0A9N4
Molecular weight:
28204
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in [formate-C-acetyltransferase]-activating enzyme activity
Specific function:
Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
nrdG
Uniprot ID:
P0A9N8
Molecular weight:
17446
General function:
Involved in electron carrier activity
Specific function:
Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin
Gene Name:
trxC
Uniprot ID:
P0AGG4
Molecular weight:
15555
Reactions
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism
Gene Name:
bioB
Uniprot ID:
P12996
Molecular weight:
38648
Reactions
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in methionine synthase activity
Specific function:
Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate
Gene Name:
metH
Uniprot ID:
P13009
Molecular weight:
135996
Reactions
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin
Gene Name:
bisC
Uniprot ID:
P20099
Molecular weight:
85850
General function:
Involved in 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
Specific function:
Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation
Gene Name:
metE
Uniprot ID:
P25665
Molecular weight:
84673
Reactions
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl- methionine. Probably responsible for the translocation of the substrate across the membrane
Gene Name:
metI
Uniprot ID:
P31547
Molecular weight:
23256
General function:
Involved in catalytic activity
Specific function:
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein
Gene Name:
lplA
Uniprot ID:
P32099
Molecular weight:
37926
Reactions
ATP + lipoate = diphosphate + lipoyl-AMP.
Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP.
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX
Gene Name:
hemN
Uniprot ID:
P32131
Molecular weight:
52729
Reactions
Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in iron-sulfur cluster binding
Specific function:
Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflC
Uniprot ID:
P32675
Molecular weight:
32429
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Not Available
Gene Name:
yggW
Uniprot ID:
P52062
Molecular weight:
42584
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for lipA
Gene Name:
lipA
Uniprot ID:
P60716
Molecular weight:
36071
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in oxidoreductase activity
Specific function:
Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
ybiY
Uniprot ID:
P75794
Molecular weight:
33038
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Catalyzes methyl transfer from S-methylmethionine or S- adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine
Gene Name:
mmuM
Uniprot ID:
Q47690
Molecular weight:
33422
Reactions
S-methyl-L-methionine + L-homocysteine = 2 L-methionine.
General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in formyl-L-methionine transport
Gene Name:
metN
Uniprot ID:
P30750
Molecular weight:
37788
General function:
Involved in catalytic activity
Specific function:
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S
Gene Name:
thiG
Uniprot ID:
P30139
Molecular weight:
26896
Reactions
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated cleavage of tyrosine to dehydroglycine and p-cresol
Gene Name:
thiH
Uniprot ID:
P30140
Molecular weight:
43320
Reactions
L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H(+).
General function:
Inorganic ion transport and metabolism
Specific function:
This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system
Gene Name:
metQ
Uniprot ID:
P28635
Molecular weight:
29432
General function:
Involved in thiamine biosynthetic process
Specific function:
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction
Gene Name:
thiC
Uniprot ID:
P30136
Molecular weight:
70850
Reactions
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO.
General function:
Involved in electron carrier activity
Specific function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions
Gene Name:
trxA
Uniprot ID:
P0AA25
Molecular weight:
11807
General function:
Not Available
Specific function:
Not Available
Gene Name:
yncA
Uniprot ID:
P76112
Molecular weight:
Not Available
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA)
Gene Name:
queA
Uniprot ID:
P0A7F9
Molecular weight:
39430
Reactions
S-adenosylmethionine + 7-aminomethyl-7-deazaguanosine = methionine + adenine + epoxyqueuosine.
General function:
Involved in 4 iron, 4 sulfur cluster binding
Specific function:
Specifically methylates position 2 of adenine 2503 in 23S rRNA
Gene Name:
rlmN
Uniprot ID:
P36979
Molecular weight:
43085
Reactions
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA.
General function:
tRNA methylthiolation
Specific function:
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Gene Name:
miaB
Uniprot ID:
P0AEI1
Molecular weight:
53662
Reactions
N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-methylthio-N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
General function:
RNA modification
Specific function:
Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12.
Gene Name:
rimO
Uniprot ID:
P0AEI4
Molecular weight:
49581
Reactions
L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine

Transporters

General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl- methionine. Probably responsible for the translocation of the substrate across the membrane
Gene Name:
metI
Uniprot ID:
P31547
Molecular weight:
23256
General function:
Involved in nucleotide binding
Specific function:
Probably part of a binding-protein-dependent transport system yecCS for an amino acid. Probably responsible for energy coupling to the transport system
Gene Name:
yecC
Uniprot ID:
P37774
Molecular weight:
27677
General function:
Involved in transporter activity
Specific function:
Probably part of the binding-protein-dependent transport system yecCS for an amino acid; probably responsible for the translocation of the substrate across the membrane
Gene Name:
yecS
Uniprot ID:
P0AFT2
Molecular weight:
24801
General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in formyl-L-methionine transport
Gene Name:
metN
Uniprot ID:
P30750
Molecular weight:
37788
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Inorganic ion transport and metabolism
Specific function:
This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system
Gene Name:
metQ
Uniprot ID:
P28635
Molecular weight:
29432
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368