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Escherichia coli K-12 substr. MG1655 Compound: L-lysine

Abbrev Name: lys

Synonyms: K, lysine, L-lys, lys, 2,6-diaminohexanoic acid, lysine acid

Superclasses: an acid all carboxy acids a carboxylate an amino acid a basic amino acid
an acid all carboxy acids a carboxylate an amino acid a polar amino acid a positively-charged polar amino acid
an acid all carboxy acids a carboxylate an amino acid an alpha amino acid a non-standard alpha amino acid an L-lysine or meso-2,6-diaminoheptanedioate
an acid all carboxy acids a carboxylate an amino acid an alpha amino acid a standard alpha amino acid
an acid all carboxy acids a carboxylate an amino acid an L-amino acid
an amino acid or its derivative an amino acid a basic amino acid
an amino acid or its derivative an amino acid a polar amino acid a positively-charged polar amino acid
an amino acid or its derivative an amino acid an alpha amino acid a non-standard alpha amino acid an L-lysine or meso-2,6-diaminoheptanedioate
an amino acid or its derivative an amino acid an alpha amino acid a standard alpha amino acid
an amino acid or its derivative an amino acid an L-amino acid

Component of: ArgP-lysine

Chemical Formula: C6H15N2O2

Molecular Weight: 147.2 Daltons

Monoisotopic Molecular Weight: 146.105527704 Daltons

L-lysine compound structure

pKa 1: 2.2

pKa 2: 8.9

pKa 3: 10.28

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

InChI: InChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/p+1/t5-/m0/s1

InChIKey: InChIKey=KDXKERNSBIXSRK-YFKPBYRVSA-O

Unification Links: CAS:56-87-1 , ChEBI:32551 , HMDB:HMDB00182 , IAF1260:33655 , KEGG:C00047 , MetaboLights:MTBLC32551 , PubChem:5460926

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -84.04

Reactions known to consume the compound:

aminopropylcadaverine biosynthesis , L-lysine degradation I :
L-lysine + H+ → CO2 + cadaverine

tRNA charging :
L-lysine + a tRNAlys + ATP + H+ → an L-lysyl-[tRNAlys] + AMP + diphosphate

Not in pathways:
a cytidine34 in tRNAIle2 + L-lysine + ATP → a lysidine34 in tRNAIle2 + AMP + diphosphate + 2 H+

Reactions known to produce the compound:

L-lysine biosynthesis I :
meso-diaminopimelate + H+L-lysine + CO2

Not in pathways:
a peptide with an N-terminal X-L-proline + H2O → a standard α amino acid + a peptide with an N-terminal L-proline + H+
a peptide + H2O → a standard α amino acid + a peptide
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a standard α amino acid + a peptide
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with an N-terminal L-aspartate + H2O → L-aspartate + a standard α amino acid
a tripeptide + H2O → a dipeptide + a standard α amino acid
a dipeptide with proline at the C-terminal + H2O → L-proline + a standard α amino acid
a dipeptide + H2O → 2 a standard α amino acid

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

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+

Reactions known to both consume and produce the compound:

fructoselysine and psicoselysine degradation :
fructoselysine 6-phosphate + H2O ↔ β-D-glucose 6-phosphate + L-lysine

In Reactions of unknown directionality:

Not in pathways:
ArgP + L-lysine = ArgP-lysine
L-lysine = (R)-β-lysine

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid

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

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

In Transport reactions:
L-lysine[periplasmic space] + H+[periplasmic space]L-lysine[cytosol] + H+[cytosol] ,
cadaverine[cytosol] + L-lysine[periplasmic space] → cadaverine[periplasmic space] + L-lysine[cytosol] ,
L-lysine[periplasmic space] + ATP + H2O → L-lysine[cytosol] + ADP + phosphate + H+ ,
L-lysine[cytosol]L-lysine[periplasmic space]

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

Inhibitor (Competitive) of: arginine decarboxylase, degradative [Blethen68] , cadaverine:H+ symporter [Soksawatmaekhin04]

Inhibitor (Noncompetitive) of: homoserine kinase [Chassagnole01]

Inhibitor (Allosteric) of: aspartate kinase [Kotaka06, Chassagnole01]

Inhibitor (Mechanism unknown) of: acetolactate synthase [Gollop82] , acetohydroxybutanoate synthase [Gollop82] , aspartate kinase [Stadtman61] , diaminopimelate decarboxylase [White65]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: Ap4A synthetase , Ap3A synthetase

This compound has been characterized as an alternative substrate of the following enzymes: leucine efflux transporter

In Growth Media: Neidhardt EZ rich defined medium , ATCC medium 57 , PMA nitrogen source test + lys , PMA carbon source test + lys


References

Blethen68: Blethen SL, Boeker EA, Snell EE (1968). "Argenine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme." J Biol Chem 1968;243(8);1671-7. PMID: 4870599

Chassagnole01: Chassagnole C, Rais B, Quentin E, Fell DA, Mazat JP (2001). "An integrated study of threonine-pathway enzyme kinetics in Escherichia coli." Biochem J 356(Pt 2);415-23. PMID: 11368768

Gollop82: Gollop N, Tavori H, Barak Z (1982). "Acetohydroxy acid synthase is a target for leucine containing peptide toxicity in Escherichia coli." J Bacteriol 149(1);387-90. PMID: 7033214

Kotaka06: Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK (2006). "Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine." J Biol Chem 281(42);31544-52. PMID: 16905770

Soksawatmaekhin04: Soksawatmaekhin W, Kuraishi A, Sakata K, Kashiwagi K, Igarashi K (2004). "Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli." Mol Microbiol 51(5);1401-12. PMID: 14982633

Stadtman61: Stadtman, E.R., Cohen, G.N., LeBras, G., Robichon-Szulmajster, H. (1961). "Feed-back Inhibition and Repression of Aspartokinase Activity in Escherichia coli and Saccharomyces cerevisiae." J. Biol. Chem.

White65: White PJ, Kelly B (1965). "Purification and properties of diaminopimelate decarboxylase from Escherichia coli." Biochem J 96;75-84. PMID: 14343156


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Jul 3, 2015, biocyc11.