Escherichia coli K-12 substr. MG1655 Compound: seleno-L-methionine

Abbrev Name: SeMet

Synonyms: selenium L-methionine

Superclasses: an acidall carboxy acidsa carboxylatean amino acida modified amino acid
an amino acid or its derivativean amino acida modified amino acid

Chemical Formula: C5H11NO2Se

Molecular Weight: 196.11 Daltons

Monoisotopic Molecular Weight: 198.00332543460001 Daltons

seleno-L-methionine compound structure

SMILES: C[Se]CCC(C([O-])=O)[N+]

InChI: InChI=1S/C5H11NO2Se/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1


Unification Links: CAS:1464-42-2, ChEBI:62621, HMDB:HMDB03966, KEGG:C05335, MetaboLights:MTBLC62621, PubChem:53262363

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -84.68

Reactions known to produce the compound:

Not in pathways:
a carboxylic ester + H2O → an alcohol + a carboxylate + H+
an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+
an acyl phosphate + H2O → a carboxylate + phosphate + H+
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 1-acyl 2-lyso-phosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+

In Reactions of unknown directionality:

Not in pathways:
a 5-L-glutamyl-[peptide][periplasm] + an amino acid[periplasm] = a 5-L-glutamyl-amino acid[periplasm] + a peptide[periplasm]

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:
an amino acid[periplasm]an amino acid[extracellular space]

Enzymes inhibited by seleno-L-methionine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: methionine transport [Kadner77]

This compound has been characterized as an alternative substrate of the following enzymes: methionine adenosyltransferase


Kadner77: Kadner RJ (1977). "Transport and utilization of D-methionine and other methionine sources in Escherichia coli." J Bacteriol 129(1);207-16. PMID: 318639

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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