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

Abbrev Name: ala

Synonyms: alanine, L-α-alanine, ala

Superclasses: an amino acid or its derivative an amino acid a neutral amino acid
an amino acid or its derivative an amino acid a non-polar amino acid
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: AlaS-L-alanine

Chemical Formula: C3H7NO2

Molecular Weight: 89.094 Daltons

Monoisotopic Molecular Weight: 89.0476784741 Daltons

L-alanine compound structure

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

InChI: InChI=1S/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1

InChIKey: InChIKey=QNAYBMKLOCPYGJ-REOHCLBHSA-N

Unification Links: CAS:56-41-7 , ChEBI:57972 , HMDB:HMDB00161 , IAF1260:33629 , KEGG:C00041 , MetaboLights:MTBLC57972 , PubChem:7311724

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -88.67

Reactions known to consume the compound:

8-amino-7-oxononanoate biosynthesis I :
a pimeloyl-[acp] + L-alanine + H+ → 8-amino-7-oxononanoate + CO2 + a holo-[acyl-carrier protein]

tRNA charging :
a tRNAala + L-alanine + ATP + H+ → an L-alanyl-[tRNAala] + AMP + diphosphate

UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-DAP-containing) :
L-alanine + UDP-N-acetyl-α-D-muramate + ATP → UDP-N-acetyl-α-D-muramoyl-L-alanine + ADP + phosphate + H+

Not in pathways:
L-alanine + pimeloyl-CoA + H+ → CO2 + 8-amino-7-oxononanoate + coenzyme A

Reactions known to produce the compound:

L-alanine biosynthesis III , molybdenum cofactor biosynthesis , thiazole biosynthesis I (E. coli) :
an [L-cysteine desulfurase]-L-cysteine + L-cysteine → an [L-cysteine desulfurase] L-cysteine persulfide + L-alanine

muropeptide degradation :
L-alanyl-L-glutamate + H2O → L-alanine + L-glutamate

Not in pathways:
L-alanyl-L-aspartate + H2O → L-alanine + L-aspartate
L-alanyl-L-glutamine + H2O → L-alanine + L-glutamine
L-alanyl-glycine + H2O → L-alanine + glycine
L-alanyl-L-histidine + H2O → L-alanine + L-histidine
L-alanyl-L-leucine + H2O → L-alanine + L-leucine
L-alanyl-L-threonine + H2O → L-alanine + L-threonine
L-methionyl-L-alanine dipeptide + H2O → L-methionine + L-alanine
L-cysteine + an unsulfurated [sulfur carrier] → L-alanine + a sulfurated [sulfur carrier]

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

Reactions known to both consume and produce the compound:

L-alanine biosynthesis I :
pyruvate + L-valine ↔ L-alanine + 3-methyl-2-oxobutanoate
L-alanine ↔ D-alanine

L-alanine biosynthesis II :
2-oxoglutarate + L-alanine ↔ L-glutamate + pyruvate

L-alanine degradation I :
L-alanine ↔ D-alanine

In Reactions of unknown directionality:

Not in pathways:
ThiS-COAMP + L-cysteine = ThiS-COSH + L-alanine + AMP
3-sulfinoalanine + H2O = L-alanine + sulfite + H+
a ThiI sulfur-carrier protein + L-cysteine = an S-sulfanyl-[ThiI sulfur-carrier protein] + L-alanine
L-selenocysteine + an unknown reduced electron acceptor = L-alanine + selenide + an unknown oxidized electron acceptor + 2 H+
L-cystein desulfurase + L-cysteine = an S-sulfanyl-[L-cysteine desulfurase] + L-alanine
alanyl-tRNA synthetase + L-alanine = AlaS-L-alanine

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]

In Transport reactions:
Na+[periplasmic space] + L-alanine[periplasmic space] → Na+[cytosol] + L-alanine[cytosol] ,
L-alanine[periplasmic space] + H+[periplasmic space]L-alanine[cytosol] + H+[cytosol] ,
L-alanine[cytosol]L-alanine[periplasmic space] ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

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

Inhibitor (Competitive) of: glutamine synthetase [Woolfolk67, Bender77, Dahlquist75]

Inhibitor (Mechanism unknown) of: L-proline:H+ symporter [MacMillan99] , serine acetyltransferase [Hindson03] , 2-dehydro-3-deoxyphosphoheptonate aldolase

This compound has been characterized as an alternative substrate of the following enzymes: D-alanine transaminase , transport of L-leucine , transport of a dipeptide

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

Transcription Units regulated by related protein AlaS-L-alanine (1 total):

Transcription-unit diagram


References

Bender77: Bender RA, Janssen KA, Resnick AD, Blumenberg M, Foor F, Magasanik B (1977). "Biochemical parameters of glutamine synthetase from Klebsiella aerogenes." J Bacteriol 129(2);1001-9. PMID: 14104

Dahlquist75: Dahlquist FW, Purich DL (1975). "Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme." Biochemistry 14(9);1980-9. PMID: 235974

Hindson03: Hindson VJ, Shaw WV (2003). "Random-order ternary complex reaction mechanism of serine acetyltransferase from Escherichia coli." Biochemistry 42(10);3113-9. PMID: 12627979

MacMillan99: MacMillan SV, Alexander DA, Culham DE, Kunte HJ, Marshall EV, Rochon D, Wood JM (1999). "The ion coupling and organic substrate specificities of osmoregulatory transporter ProP in Escherichia coli." Biochim Biophys Acta 1420(1-2);30-44. PMID: 10446288

Woolfolk67: Woolfolk CA, Stadtman ER (1967). "Regulation of glutamine synthetase. 3. Cumulative feedback inhibition of glutamine synthetase from Escherichia coli." Arch Biochem Biophys 118(3);736-55. PMID: 4860415


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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 Sat Apr 25, 2015, biocyc12.