Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references
Chemical compound
Histidine (symbol His or H)[2] is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also.[3] It is encoded by the codons CAU and CAC.
Histidine was first isolated by Albrecht Kossel and Sven Gustaf Hedin in 1896.[4] The name stems from its discovery in tissue, from ἱστόςhistós "tissue".[2] It is also a precursor to histamine, a vital inflammatory agent in immune responses. The acyl radical is histidyl.
^ ab"Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.
^Kopple, J D; Swendseid, M E (1975). "Evidence that histidine is an essential amino acid in normal and chronically uremic man". Journal of Clinical Investigation. 55 (5): 881–91. doi:10.1172/JCI108016. PMC 301830. PMID 1123426.
^Vickery, Hubert Bradford; Leavenworth, Charles S. (1928-08-01). "On the Separation of Histidine and Arginine" (PDF). Journal of Biological Chemistry. 78 (3): 627–635. doi:10.1016/S0021-9258(18)83967-9. ISSN 0021-9258.
Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated...
Carnosine (beta-alanyl-L-histidine) is a dipeptide molecule, made up of the amino acids beta-alanine and histidine. It is highly concentrated in muscle...
In enzymology, a histidine transaminase (EC 2.6.1.38) is an enzyme that catalyzes the chemical reaction L-histidine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons...
enzyme histidine decarboxylase (EC 4.1.1.22, HDC) is transcribed on chromosome 15, region q21.1-21.2, and catalyzes the decarboxylation of histidine to form...
Histidine phosphotransfer domains and histidine phosphotransferases (both often abbreviated HPt) are protein domains involved in the "phosphorelay" form...
Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play...
Ergothioneine is a naturally occurring amino acid and is a thiourea derivative of histidine, containing a sulfur atom on the imidazole ring. This compound occurs...
isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine. Six other amino acids are considered conditionally essential...
muscle and brain of mammals and birds. The pKa of the imidazole ring of histidine, when contained in anserine, is 7.04. An animal model study of Alzheimer's...
Histidine methyl ester (HME) is an irreversible histidine decarboxylase inhibitor. It is the methyl ester of histidine. Histidine decarboxylase α-Fluoromethylhistidine...
repression or derepression of histidine synthesis is the concentration of histidine charged tRNAs. The regulation of histidine is actually quite simple considering...
dictionary. Protein histidine kinase may refer to: Histidine kinase, an enzyme Protein-histidine tele-kinase, an enzyme Protein-histidine pros-kinase, an...
Histidine triad nucleotide-binding protein 1 also known as adenosine 5'-monophosphoramidase is an enzyme that in humans is encoded by the HINT1 gene....
and histidine (His, H). Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7. Histidine's imidazole...
peptide histidine isoleucine, is a peptide which functions as a hormone. This peptide contains a composition of 27 amino acids with histidine on the N-terminus...
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