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Fixed the wrong structure of which had incorrect linkage with the ring in histidine Tags: Visual edit Mobile edit Mobile web edit |
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{{short description|Chemical compound}}
{{chembox
| Name =
| ImageFile1_Ref = {{chemboximage|correct|??}}
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| ImageFileL2 = Histidine-from-xtal-3D-bs-17.png
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| OtherNames = 2-Amino-3-(1''H''-imidazol-4-yl)propanoic acid
| Section1 = {{Chembox Identifiers
| CASNo = 71-00-1▼
| IUPHAR_ligand = 3310▼
| CASNo_Ref = {{cascite|correct|CAS}}▼
| Beilstein = 84088
| ChEMBL_Ref = {{ebicite|correct|EBI}}▼
| ChEMBL = 17962▼
| ChEBI_Ref = {{ebicite|correct|EBI}}▼
| ChEBI = 15971▼
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID = 6038
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = 4QD397987E
| EINECS = 200-745-3
| Gmelin = 83042
▲| IUPHAR_ligand = 3310
| KEGG_Ref = {{keggcite|correct|kegg}}
| KEGG = D00032
▲| ChEMBL_Ref = {{ebicite|correct|EBI}}
▲| ChEMBL = 17962
▲| ChEBI_Ref = {{ebicite|correct|EBI}}
▲| ChEBI = 15971
| SMILES = O=C([C@H](CC1=CNC=N1)N)O
| SMILES1 = O=C([C@H](CC1=CNC=N1)[NH3+])[O-]
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| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = HNDVDQJCIGZPNO-YFKPBYRVSA-N
▲| CASNo = 71-00-1
▲| CASNo_Ref = {{cascite|correct|CAS}}
| PubChem = 6274
| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
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| AutoignitionPt = }}
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'''Histidine''' (symbol '''His''' or '''H''')<ref name=":7">{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 | url-status = dead }}</ref> is an
Histidine was first isolated by
▲'''Histidine''' (symbol '''His''' or '''H''')<ref>{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 | url-status = dead }}</ref> is an essential [[Amino acid|α-amino acid]] that is used in the biosynthesis of [[protein]]s. It contains an [[Amine|α-amino group]] (which is in the [[protonated]] –NH<sub>3</sub><sup>+</sup> form under [[Physiological condition|biological conditions]]), a [[carboxylic acid]] group (which is in the deprotonated –COO<sup>−</sup> 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 amino acid|essential]] only for infants, it has now been shown in longer-term studies to be essential for adults also.<ref>{{cite journal |doi=10.1172/JCI108016 |title=Evidence that histidine is an essential amino acid in normal and chronically uremic man |year=1975 |last1=Kopple |first1=J D |last2=Swendseid |first2=M E |journal=Journal of Clinical Investigation |volume=55 |issue=5 |pages=881–91 |pmid=1123426 |pmc=301830}}</ref> It is [[Genetic code|encoded]] by the [[Genetic code|codons]] CAU and CAC.
▲Histidine was first isolated by German physician [[Albrecht Kossel]] and [[Sven Gustaf Hedin]] in 1896.<ref>{{Cite journal|last1=Vickery|first1=Hubert Bradford|last2=Leavenworth|first2=Charles S.|title=On the Separation of Histidine and Arginine|date=1928-08-01|url=http://www.jbc.org/content/78/3/627.full.pdf|journal=Journal of Biological Chemistry|language=en|volume=78|issue=3|pages=627–635|doi=10.1016/S0021-9258(18)83967-9|issn=0021-9258|doi-access=free}}</ref> It is also a [[Precursor (chemistry)|precursor]] to [[histamine]], a vital inflammatory agent in immune responses. The acyl [[radical (chemistry)|radical]] is '''histidyl'''.
==Properties of the imidazole side chain==
The conjugate acid (protonated form) of the [[imidazole]] [[side chain]] in histidine has a [[Acid dissociation constant|p''K''<sub>a</sub>]] of approximately 6.0. Thus, below a pH of 6, the imidazole ring is mostly [[Protonation|protonated]] (as described by the [[Henderson–Hasselbalch equation]]). The resulting imidazolium ring bears two NH bonds and has a positive charge. The positive charge is equally distributed between both [[nitrogen]]s and can be represented with two equally important [[resonance structure]]s. Sometimes, the symbol '''Hip''' is used for this protonated form instead of the usual His.<ref name=":4" /><ref name=":5">{{Cite web |title=HISTIDINE |url=http://ambermd.org/Questions/HIS.html |access-date=2022-05-12 |website=ambermd.org}}</ref><ref name=":6">{{Cite journal |
The acid-base properties of the imidazole side chain are relevant to the [[catalyst|catalytic mechanism]] of many [[enzyme]]s.<ref name=":0">{{Cite journal|last=Ingle|first=Robert A.|title=Histidine Biosynthesis|journal=The Arabidopsis Book|volume=9|pages=e0141|doi=10.1199/tab.0141|pmc=3266711|pmid=22303266|year=2011}}</ref> In [[catalytic triad]]s, the basic nitrogen of histidine abstracts 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 anhydrase]]s, 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. In helices E and F of [[
The tautomerism and acid-base properties of the imidazole side chain has been characterized by <sup>15</sup>N NMR spectroscopy. The two <sup>15</sup>N chemical shifts are similar (about 200 ppm, relative to [[nitric acid]] on the sigma scale, on which increased shielding corresponds to increased [[chemical shift]]). [[NMR]] spectral measurements shows that the chemical shift of N1-H drops slightly, whereas the chemical shift of N3-H drops considerably (about 190 vs. 145 ppm). This change indicates that the N1-H tautomer is preferred, possibly due to hydrogen bonding to the neighboring [[ammonium]]. The shielding at N3 is substantially reduced due to the second-order [[Paramagnetism|paramagnetic]] effect, which involves a symmetry-allowed interaction between the nitrogen lone pair and the excited π* states of the [[aromatic ring]]. At pH > 9, the chemical shifts of N1 and N3 are approximately 185 and 170 ppm.<ref>{{cite book|title=ABCs of FT-NMR|last=Roberts|first=John D.|publisher=University Science Books|year=2000|isbn=978-1-891389-18-4|location=Sausalito, CA|pages=258–9}}</ref>
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===Ligand===
[[Image:Succinate Dehygrogenase 1YQ3 Haem group.png|thumb|left|The histidine-bound [[heme]] group of [[succinate dehydrogenase]], an [[electron carrier]] in the [[mitochondria]]l [[electron transfer chain]]. The large semi-transparent sphere indicates the location of the [[iron]] [[ion]]. From {{PDB|1YQ3}}.|205x205px]]
[[Image:Cu3Im8laccase.png|thumb|left|The tricopper site found in many
Histidine forms [[amino acid complex|complexes]] with many metal ions. The imidazole sidechain of the histidine residue commonly serves as a [[ligand]] in [[metalloprotein]]s. One example is the axial base attached to Fe in myoglobin and hemoglobin. Poly-histidine tags (of six or more consecutive H residues) are utilized for protein purification by binding to columns with nickel or cobalt, with micromolar affinity.<ref>{{Cite
==Metabolism==
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Histidine is synthesized from [[phosphoribosyl pyrophosphate]] (PRPP), which is made from [[ribose-5-phosphate]] by [[ribose-phosphate diphosphokinase]] in the [[pentose phosphate pathway]]. The first reaction of histidine biosynthesis is the condensation of PRPP and [[adenosine triphosphate]] (ATP) by the enzyme [[ATP phosphoribosyltransferase|ATP-phosphoribosyl transferase]]. ATP-phosphoribosyl transferase is indicated by His1 in the image.<ref name=":1" /> His4 gene product then hydrolyzes the product of the condensation, phosphoribosyl-ATP, producing phosphoribosyl-AMP (PRAMP), which is an irreversible step. His4 then catalyzes the formation of phosphoribosylformiminoAICAR-phosphate, which is then converted to phosphoribulosylformimino-AICAR-P by the His6 gene product.<ref name=":2">{{Cite journal|last1=Kulis-Horn|first1=Robert K|last2=Persicke|first2=Marcus|last3=Kalinowski|first3=Jörn|date=2014-01-01|title=Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum|journal=Microbial Biotechnology|volume=7|issue=1|pages=5–25|doi=10.1111/1751-7915.12055|issn=1751-7915|pmc=3896937|pmid=23617600}}</ref> His7 splits phosphoribulosylformimino-AICAR-P to form {{sm|d}}-erythro-imidazole-glycerol-phosphate. After, His3 forms imidazole acetol-phosphate releasing water. His5 then makes {{sm|l}}-histidinol-phosphate, which is then hydrolyzed by His2 making [[histidinol]]. [[Histidinol dehydrogenase|His4]] catalyzes the oxidation of {{sm|l}}-histidinol to form {{sm|l}}-histidinal, an amino aldehyde. In the last step, {{sm|l}}-histidinal is converted to {{sm|l}}-histidine.<ref name=":2" /><ref>{{Cite journal|last=Adams|first=E.|date=1955-11-01|title=L-Histidinal, a biosynthetic precursor of histidine|journal=The Journal of Biological Chemistry|volume=217|issue=1|pages=325–344|doi=10.1016/S0021-9258(19)57184-8|issn=0021-9258|pmid=13271397|doi-access=free}}</ref>
The histidine biosynthesis pathway has been studied in the fungus ''[[Neurospora crassa]]'', and a gene (''His-3'') encoding a [[multienzyme complex]] was found that was similar to the ''His4'' gene of the bacterium ''[[Escherichia coli|E. coli]]''.<ref name="Ahmed1968">Ahmed A. Organization of the histidine-3 region of Neurospora. Mol Gen Genet. 1968;103(2):185-93. doi: 10.1007/BF00427145. PMID 4306011</ref> A genetic study of ''N. crassa'' histidine [[mutant]]s indicated that the individual activities of the multienzyme complex occur in discrete, contiguous sections of the ''His-3'' [[gene mapping|genetic map]], suggesting that the different activities of the multienzyme complex are encoded separately from each other.<ref name = Ahmed1968/> However, mutants were also found that lacked all three activities simultaneously, suggesting that some mutations cause loss of function of the complex as a whole.
Just like animals and microorganisms, plants need histidine for their growth and development.<ref name=":0" /> Microorganisms and plants are similar in that they can synthesize histidine.<ref>{{Cite web|url=http://genetics.thetech.org/ask/ask396|title=Understanding Genetics|website=genetics.thetech.org|access-date=2016-05-19}}</ref> Both synthesize histidine from the biochemical intermediate phosphoribosyl pyrophosphate. In general, the histidine biosynthesis is very similar in plants and microorganisms.<ref>{{Cite journal|last1=Stepansky|first1=A.|last2=Leustek|first2=T.|date=2006-03-01|title=Histidine biosynthesis in plants|journal=Amino Acids|volume=30|issue=2|pages=127–142|doi=10.1007/s00726-005-0247-0|issn=0939-4451|pmid=16547652|s2cid=23733445}}</ref>▼
▲Just like animals and microorganisms, plants need histidine for their growth and development.<ref name=":0" /> Microorganisms and plants are similar in that they can synthesize histidine.<ref>{{
==== Regulation of biosynthesis ====
This pathway requires energy in order to occur therefore, the presence of ATP activates the first enzyme of the pathway, ATP-phosphoribosyl transferase (shown as His1 in the image on the right). ATP-phosphoribosyl transferase is the rate determining enzyme, which is regulated through feedback inhibition meaning that it is inhibited in the presence of the product, histidine.<ref>{{Cite journal|last1=Cheng|first1=Yongsong|last2=Zhou|first2=Yunjiao|last3=Yang|first3=Lei|last4=Zhang|first4=Chenglin|last5=Xu|first5=Qingyang|last6=Xie|first6=Xixian|last7=Chen|first7=Ning|date=2013-05-01|title=Modification of histidine biosynthesis pathway genes and the impact on production of L-histidine in Corynebacterium glutamicum|journal=Biotechnology Letters|volume=35|issue=5|pages=735–741|doi=10.1007/s10529-013-1138-1|issn=1573-6776|pmid=23355034|s2cid=18380727}}</ref>
=== Degradation ===
Histidine is one of the amino acids that can be converted to intermediates of the tricarboxylic acid (TCA) cycle (also known as the citric acid cycle).<ref name=":3">Board review series (BRS)-- Biochemistry, Molecular Biology, and Genetics (fifth edition): Swanson, Kim, Glucksman</ref> Histidine, along with other amino acids such as proline and arginine, takes part in deamination, a process in which its amino group is removed. In [[prokaryote]]s, histidine is first converted to urocanate by histidase. Then, urocanase converts urocanate to 4-imidazolone-5-propionate. Imidazolonepropionase catalyzes the reaction to form [[formiminoglutamate]] (FIGLU) from 4-imidazolone-5-propionate.<ref>{{Cite journal|last1=Coote|first1=J. G.|last2=Hassall|first2=H.|date=1973-03-01|title=The degradation of l-histidine, imidazolyl-l-lactate and imidazolylpropionate by Pseudomonas testosteroni|journal=Biochemical Journal|volume=132|issue=3|pages=409–422|issn=0264-6021|pmc=1177604|pmid=4146796|doi=10.1042/bj1320409}}</ref> The formimino group is transferred to [[tetrahydrofolate]], and the remaining five carbons form glutamate.<ref name=":3" /> Overall, these reactions result in the formation of glutamate and ammonia.<ref>{{Cite journal|last1=Mehler|first1=A. H.|last2=Tabor|first2=H.|date=1953-04-01|title=Deamination of histidine to form urocanic acid in liver|journal=The Journal of Biological Chemistry|volume=201|issue=2|pages=775–784|doi=10.1016/S0021-9258(18)66234-9|issn=0021-9258|pmid=13061415|doi-access=free}}</ref> Glutamate can then be deaminated by [[glutamate dehydrogenase]] or transaminated to form α-ketoglutarate.<ref name=":3" />
=== Conversion to other biologically active amines ===
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==Requirements==
The [[Food and Nutrition Board]] (FNB) of the [[U.S. Institute of Medicine]] set [[Recommended Dietary Allowances]] (RDAs) for [[essential amino acid]]s in 2002. For histidine, for adults 19 years and older, 14 mg/kg body weight/day.<ref name="DRItext">{{cite book | last1 = Institute of Medicine | title = Dietary Reference Intakes for Energy, Carbohydrates, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids | chapter = Protein and Amino Acids | publisher = The National Academies Press | year = 2002 | location = Washington, DC | pages = 589–768 | doi = 10.17226/10490 | isbn = 978-0-309-08525-0 | chapter-url = https://www.nap.edu/read/10490/chapter/12| author1-link = Institute of Medicine }}</ref> Supplemental histidine is being investigated for use in a variety of different conditions, including neurological disorders, atopic dermatitis, metabolic syndrome, diabetes, uraemic anaemia, ulcers, inflammatory bowel diseases, malignancies, and muscle performance during strenuous exercise.<ref>{{Cite journal |last=Holeček |first=Milan |date=2020-03-22 |title=Histidine in Health and Disease: Metabolism, Physiological Importance, and Use as a Supplement |journal=Nutrients |volume=12 |issue=3 |pages=848 |doi=10.3390/nu12030848 |issn=2072-6643 |pmc=7146355 |pmid=32235743|doi-access=free }}</ref>
== See also ==
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== External links ==
*[http://gmd.mpimp-golm.mpg.de/Spectrums/a4fc4f0c-0812-4f61-94fd-a79c61419670.aspx Histidine MS Spectrum]
{{Amino acids}}
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[[Category:Proteinogenic amino acids]]
[[Category:Alpha-Amino acids]]
[[Category:Basic amino acids]]
[[Category:Essential amino acids]]
[[Category:Imidazoles]]
[[Category:Carbonic anhydrase activators]] <!--https://www.ncbi.nlm.nih.gov/pubmed/29478330-->
[[Category:Aromatic amino acids]]
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