Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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

Abbrev Name: his

Synonyms: glyoxaline-5-alanine, α-amino-4-imidazoleproprionic acid, (S)-α-amino-1H-imidazole-4-propanoic acid, H, histidine, his, L-his

Superclasses: 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 standard alpha amino acid
an amino acid or its derivative an amino acid an aromatic amino acid an aromatic L-amino acid
an amino acid or its derivative an amino acid an L-amino acid an aromatic L-amino acid
an amino acid or its derivative an amino acid an L-amino acid

Chemical Formula: C6H9N3O2

Molecular Weight: 155.16 Daltons

Monoisotopic Molecular Weight: 155.0694765487 Daltons

SMILES: C1(NC=NC=1CC(C(=O)[O-])[N+])

InChI: InChI=1S/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1

InChIKey: InChIKey=HNDVDQJCIGZPNO-YFKPBYRVSA-N

Unification Links: CAS:71-00-1 , ChEBI:57595 , HMDB:HMDB00177 , IAF1260:33985 , KEGG:C00135 , MetaboLights:MTBLC57595 , PubChem:6971009

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -57.44

Reactions known to consume the compound:

tRNA charging :
tRNAhis + L-histidine + ATP + H+ → L-histidyl-tRNAhis + AMP + diphosphate

Reactions known to produce the compound:

histidine biosynthesis :
histidinal + NAD+ + H2O → L-histidine + NADH + 2 H+

Not in pathways:
L-alanyl-L-histidine + H2O → L-alanine + L-histidine


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
amino acids(n) + H2O → a standard α amino acid + amino acids(n-1)
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with L-aspartate at the N-terminal + 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


a polypeptide + H2O → a polypeptide + an L-amino acid

Reactions known to both consume and produce the compound:

Not in pathways:
an aromatic amino acid + 2-oxoglutarate ↔ an aromatic oxo-acid + L-glutamate

In Reactions of unknown directionality:

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


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:
ATP + L-histidine[periplasmic space] + H2O → ADP + L-histidine[cytosol] + phosphate + H+ ,
an aromatic amino acid[cytosol]an aromatic amino acid[periplasmic space] ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

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

Inhibitor (Competitive) of: histidinol-phosphatase [Brady73]

Inhibitor (Allosteric) of: ATP phosphoribosyltransferase [Tebar76]

Inhibitor (Mechanism unknown) of: glutamine synthetase [Woolfolk67, Bender77, Comment 1]

In Growth Media: Neidhardt EZ rich defined medium , Davis and Mingioli medium A , PMA nitrogen source test + his , PMA carbon source test + his , M56 medium


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

Brady73: Brady DR, Houston LL (1973). "Some properties of the catalytic sites of imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase, a bifunctional enzyme from Salmonella typhimurium." J Biol Chem 1973;248(7);2588-92. PMID: 4349042

Tebar76: Tebar AR, Ballesteros AO (1976). "Kinetic properties of ATP phosphoribosyltransferase of Escherichia coli." Mol Cell Biochem 11(3);131-6. PMID: 781521

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


Report Errors or Provide Feedback
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 18.5 on Tue Nov 25, 2014, BIOCYC13A.