Histidine

NatOrganicBox


name=2-amino-3-(3H-imidazol-4-yl)propanoic acid
synonyms=Imidazole alanine
PubChem = 773
CAS = 71-00-1
SMILES = N [C@@H] (Cc1 [nH] cnc1)C(O)=O
C=6 | H=9 | N=3 | O=2
mass=155.16 g/mol

Histidine (abbreviated as His or H) [cite web | author=IUPAC-IUBMB Joint Commission on Biochemical Nomenclature | title=Nomenclature and Symbolism for Amino Acids and Peptides | work=Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc | url=http://www.chem.qmul.ac.uk/iupac/AminoAcid/ | accessdate=2007-05-17] is one of the 20 standard amino acids present in proteins. In the nutritional sense, in humans, histidine is considered an essential amino acid, but mostly only in children. Its codons are CAU and CAC.

Histidine was first isolated by German physician Albrecht Kossel in 1896.

Chemical properties

The imidazole side chains and the relatively neutral pKa of histidine (ca 6.0) mean that relatively small shifts in cellular pH will change its charge. For this reason, this amino acid side chain finds its way into considerable use as a coordinating ligand in metalloproteins, and also as a catalytic site in certain enzymes. The imidazole side chain has two nitrogens with different properties: One is bound to hydrogen and donates its lone pair to the aromatic ring and as such is slightly acidic, whereas the other one donates only one electron to the ring so it has a free lone pair and is basic. These properties are exploited in different ways in proteins. In catalytic triads, the basic nitrogen of histidine is used to abstract a proton from serine, threonine or cysteine to activate it as a nucleophile. In a histidine proton shuttle, histidine is used to quickly shuttle protons, it can do this by abstracting a proton with its basic nitrogen to make a positively-charged intermediate and then use another molecule, a buffer, to extract the proton from its acidic nitrogen. In carbonic anhydrases, a histidine proton shuttle is utilized to rapidly shuttle protons away from a zinc-bound water molecule to quickly regenerate the active form of the enzyme.

Metabolism

The amino acid is a precursor for histamine and carnosine biosynthesis.

The enzyme histidine ammonia-lyase converts histidine into ammonia and urocanic acid. A deficiency in this enzyme is present in the rare metabolic disorder histidinemia.

=Additional

References

See also

*Aromatic amino acids
*Urocanic aciduria
*Carnosinemia
*Beta-alanine

External links

* [http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/His1.html Histidine biosynthesis (early stages)]
* [http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/His2.html Histidine biosynthesis (later stages)]
* [http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/His3.html Histidine catabolism]
* [http://www.compchemwiki.org/index.php?title=Histidine Computational Chemistry Wiki]