Histidine

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Chemical structure of Histidine

Chemical structure of Histidine

Histidine

Systematic (IUPAC) name
2-amino-3-(3H-imidazol-4-yl)propanoic acid
Identifiers
CAS number 71-00-1
PubChem         773
Chemical data
Formula C6H9N3O2 
Molar mass 155.16 g/mol
SMILES N[C@@H](Cc1[nH]cnc1)C(O)=O
Complete data

Histidine (abbreviated as His or H)[1] is one of the 20 most common natural 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 pair 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.

Because of histidine's affinity for metal ions, researchers will often add a polyhistidine-tag to a protein of interest. The metal affinity can then be used to purify, detect, or immobilize the protein to be studied.

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 images

References

  1. IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17. 

External links


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Major families of biochemicals</td></tr><tr><td colspan="3" style="text-align: center;">Peptides | Amino acids | Nucleic acids | Carbohydrates | Nucleotide sugars | Lipids | Terpenes | Carotenoids | Tetrapyrroles | Enzyme cofactors | Steroids | Flavonoids | Alkaloids | Polyketides | Glycosides</td></tr><tr bgcolor="pink"><td style="white-space: nowrap; width: 10%; color: pink;">Analogues of nucleic acids:</td><td align="center">The 20 Common Amino Acids ("dp" = data page)</td><td style="white-space: nowrap; width: 10%; color: pink;">Analogues of nucleic acids:</td></tr>
Alanine (dp) | Arginine (dp) | Asparagine (dp) | Aspartic acid (dp) | Cysteine (dp) | Glutamic acid (dp) | Glutamine (dp) | Glycine (dp) | Histidine (dp) | Isoleucine (dp) | Leucine (dp) | Lysine (dp) | Methionine (dp) | Phenylalanine (dp) | Proline (dp) | Serine (dp) | Threonine (dp) | Tryptophan (dp) | Tyrosine (dp) | Valine (dp)
bs:Histidin

ca:Histidina cs:Histidin de:Histidineo:Histidinoko:히스티딘 hr:Histidin id:Histidin it:Istidina he:היסטידין lv:Histidīns lb:Histidin lt:Histidinas hu:Hisztidin nl:Histidineno:Histidinfi:Histidiini sv:Histidinuk:Гістидин


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