histidine

ヒスチジン

　

WordNet

1. an essential amino acid found in proteins that is important for the growth and repair of tissue

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/27 18:24:40」(JST)

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L-ヒスチジン
IUPAC名 Histidine
別称 2-Amino-3-(1H-imidazol-4-yl)propanoic acid
識別情報
CAS登録番号	71-00-1
PubChem	773
ChemSpider	6038
UNII	4QD397987E
KEGG	D00032
ChEMBL	CHEMBL17962
SMILES O=C(O)[C@@H](N)Cc1cncn1
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  Key: HNDVDQJCIGZPNO-YFKPBYRVSA-N  InChI=1/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 Key: HNDVDQJCIGZPNO-YFKPBYRVBM
特性
化学式	C6H9N3O2
モル質量	155.15 g mol−1
補足データページ
構造および特性	n, εr, etc.
熱力学的データ	相挙動 固体、液体、気体
スペクトルデータ	UV, IR, NMR, MS
特記なき場合、データは常温 (25 °C)・常圧 (100 kPa) におけるものである。

ヒスチジン (histidine) はアミノ酸の一種で2-アミノ-3-（1H-イミダゾ-4-イル）プロピオン酸のこと。名前はギリシャ語で「組織」という意味。

塩基性アミノ酸の一種で、必須アミノ酸。糖原性を持つ。側鎖にイミダゾイル基という複素芳香環を持ち、この部分の特殊な性質により酵素の活性中心や、蛋白質分子内でのプロトン移動に関与している。蛋白質中では金属との結合部位となり、あるいは水素結合やイオン結合を介してとしてその高次構造の維持に重要な役割を果たしている。 ヒスタミンおよびカルノシン生合成の前駆体でもある。

イミダゾイル基

窒素原子に結合したプロトン (H⁺) の着脱を起こし、塩基または非常に弱い酸として働く。また、二重結合の位置と水素原子が移動した互変異性体が平衡状態にある。いずれの構造の場合でも、水素原子を持たない側の窒素原子が容易に水素原子と反応し、同時に他方の窒素原子上にある水素原子を放出する。結果として、水素原子を運ぶ担体として機能することができる。

炭酸脱水酵素中では活性中心の亜鉛に結合した水分子からプロトンを引き抜いて活性型を再生させ、触媒三残基においてはセリン、スレオニン、システインからプロトンを引き抜き、それらを求核剤として活性化させる役割を果たす。

合成法

フルクトースとホルマリンとアンモニアからヒドロキシメチルイミダゾールを作り、この塩化物にアセトアミドマロン酸エステルを縮合して作る。

関連項目

• 金属タンパク質
• Hisタグ

外部リンク

• ヒスチジン - 「健康食品」の安全性・有効性情報 （国立健康・栄養研究所）

wiki en

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Not to be confused with histamine.

L-Histidine

Names
IUPAC name Histidine
Other names 2-Amino-3-(1H-imidazol-4-yl)propanoic acid
Identifiers
CAS Registry Number	71-00-1 Y
ChEBI	CHEBI:57595 Y
ChEMBL	ChEMBL17962 Y
ChemSpider	6038 Y
DrugBank	DB00117 Y
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 Y Key: HNDVDQJCIGZPNO-YFKPBYRVSA-N Y 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 Key: HNDVDQJCIGZPNO-YFKPBYRVSA-N
IUPHAR/BPS	3310
Jmol-3D images	Image Image
KEGG	D00032 Y
PubChem	773
SMILES O=C([C@H](CC1=CNC=N1)N)O O=C(O)[C@@H](N)Cc1c[nH]cn1
UNII	4QD397987E Y
Properties
Chemical formula	C6H9N3O2
Molar mass	155.16 g·mol−1
Solubility in water	4.19g/100g @ 25 °C
Hazards
Safety data sheet	See: data page
NFPA 704	1 1 0
Supplementary data page
Structure and properties	Refractive index (n), Dielectric constant (εr), etc.
Thermodynamic data	Phase behaviour solid–liquid–gas
Spectral data	UV, IR, NMR, MS
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Y verify (what is: Y/N?)
Infobox references

Histidine (abbreviated as His or H) is an essential, α-amino acid with an imidazole functional group. Initially thought essential only for infants, longer-term studies shown it's essential for adult humans as well. It is one of the 23 proteinogenic amino acids. Its codons are CAU and CAC. Histidine was first isolated by German physician Albrecht Kossel in 1896.

Chemical properties

The conjugate acid (protonated form) of the imidazole side chain in histidine has a pK_a of approximately 6.0. This means that, at physiologically relevant pH values, relatively small shifts in pH will change its average charge. Below a pH of 6, the imidazole ring is mostly protonated as described by the Henderson–Hasselbalch equation. When protonated, the imidazole ring bears two NH bonds and has a positive charge. The positive charge is equally distributed between both nitrogens and can be represented with two equally important resonance structures.

Aromaticity

The imidazole ring of histidine is aromatic at all pH values. It contains six pi electrons: four from two double bonds and two from a nitrogen lone pair. It can form pi stacking interactions, but is complicated by the positive charge. It does not absorb at 280 nm in either state, but does in the lower UV range more than some amino acids.

Biochemistry

The imidazole sidechain of histidine is a common coordinating ligand in metalloproteins and is a part of catalytic sites in certain enzymes. 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. Histidine is also important in haemoglobin in helices E and F. Histidine assists in stabilising oxyhaemoglobin and destabilising CO-bound haemoglobin. As a result, carbon monoxide binding is only 200 times stronger in haemoglobin, compared to 20,000 times stronger in free haem.

Certain amino acids can be converted to intermediates of the TCA cycle. Carbons from four groups of amino acids form the TCA cycle intermediates α-ketoglutarate, succinyl CoA, fumarate, and oxaloacetate. Amino acids that form α-ketoglutarate are glutamate, glutamine, proline, arginine, and histidine. Histidine is converted to formiminoglutamate (FIGLU). The formimino group is transferred to tetrahydrofolate, and the remaining five carbons form glutamate. Glutamate can be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate.

NMR

When protonated, the ¹⁵N chemical shifts of the side-chain nitrogens are similar (about 200 ppm, relative to nitric acid on the sigma scale, on which increased shielding corresponds to increased chemical shift). As the pH increases past approximately 6, the protonation of the imidazole ring is lost. The remaining proton of the now-neutral imidazole can exist on either nitrogen, giving rise to what is known as the N-1 or N-3 tautomers. NMR shows that the chemical shift of N-1 drops slightly, whereas the chemical shift of N-3 drops considerably (about 190 vs. 145 ppm). This indicates that the N-1-H tautomer is preferred, it is presumed due to hydrogen bonding to the neighboring ammonium. The shielding at N-3 is substantially reduced due to the second-order paramagnetic effect, which involves a symmetry-allowed interaction between the nitrogen lone pair and the excited pi* states of the aromatic ring. As the pH rises above 9, the chemical shifts of N-1 and N-3 become approximately 185 and 170 ppm. It is worth noting that the deprotonated form of imidazole, imidazolate ion, would be formed only above a pH of 14, and is therefore not physiologically relevant. This change in chemical shifts can be explained by the presumably decreased hydrogen bonding of an amine over an ammonium ion, and the favorable hydrogen bonding between a carboxylate and an NH. This should act to decrease the N-1-H tautomer preference.

Metabolism

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

Conversion of histidine to histamine by histidine decarboxylase

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. In Actinobacteria and filamentous fungi, such as Neurospora crassa, histidine can be converted into the antioxidant ergothioneine.

Supplementation

Supplementation of histidine has been shown to cause rapid zinc excretion in rats with an excretion rate 3 to 6 times normal.

Additional images

• Histidine

• The histidine-bound heme group of succinate dehydrogenase, an electron carrier in the mitochondrial electron transfer chain. The large semi-transparent sphere indicates the location of the iron ion. From PDB: 1YQ3 .

See also

• Imidazole
• Aromatic amino acids
• Urocanic aciduria
• Carnosinemia
• Beta-alanine
• Diphthamide
• Pauly reaction

References

External links

• Histidine MS Spectrum
• Histidine biosynthesis (early stages)
• Histidine biosynthesis (later stages)
• Histidine catabolism
• Food Sources of Histidine

UpToDate Contents

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English Journal

• Effect of methyl jasmonate application to grapevine leaves on grape amino acid content.

• Garde-Cerdán T1, Portu J2, López R2, Santamaría P2.
• Food chemistry.Food Chem.2016 Jul 15;203:536-9. doi: 10.1016/j.foodchem.2016.02.049. Epub 2016 Feb 9.
• Over the last few years, considerable attention has been paid to the application of elicitors to vineyard. However, research about the effect of elicitors on grape amino acid content is scarce. Therefore, the aim of this study was to evaluate the influence of foliar application of methyl jasmonate o
• PMID 26948648

• Discovery, structural characterization and functional analysis of alpha-2-macroglobulin, a novel immune-related molecule from Holothuria atra.

• Qian J1, Ren C2, Xia J3, Chen T4, Yu Z5, Hu C6.
• Gene.Gene.2016 Jul 10;585(2):205-15. doi: 10.1016/j.gene.2016.03.024. Epub 2016 Mar 29.
• The non-specific protease inhibitor alpha-2-macroglobulin (A2M) is a key macromolecular glycoprotein that involved in host immune defense against pathogens in vertebrates and invertebrates. However, no research regarding A2M has been developed in echinoderms to date. In this study, the full-length c
• PMID 27033585

• Mixed planting with a leguminous plant outperforms bacteria in promoting growth of a metal remediating plant through histidine synthesis.

• Adediran GA1, Ngwenya BT1, Mosselmans JF2, Heal KV1, Harvie BA1.
• International journal of phytoremediation.Int J Phytoremediation.2016 Jul 2;18(7):720-9. doi: 10.1080/15226514.2015.1131235.
• The effectiveness of plant growth promoting bacteria (PGPB) in improving metal phytoremediation is still limited by stunted plant growth under high soil metal concentrations. Meanwhile, mixed planting with leguminous plants is known to improve yield in nutrient deficient soils but the use of a metal
• PMID 26682469

Japanese Journal

• Reaction mechanism of human α-amylase : The role of chloride and histidine residues

• Ogawa Zensuke,Kitagawa Yumi,Ikeya Hitoshi [他]
• International journal of analytical bio-science 2(1), 33-40, 2014-03
• NAID 40020032359

• Characterization of a Gene Family Encoding SEA (Sea-urchin Sperm Protein, Enterokinase and Agrin)-Domain Proteins with Lectin-Like and Heme-Binding Properties from Schistosoma japonicum

• Mbanefo Evaristus Chibunna,Kikuchi Mihoko,Huy Nguyen Tien,Shuaibu Mohammed Nasir,Cherif Mahamoud Sama,Yu Chuanxin,Wakao Masahiro,Suda Yasuo,Hirayama Kenji
• PLoS Neglected Tropical Diseases 8(1), e2644, 2014-01-09
• … The heme-binding mode showed heme molecule inserted into a hydrophobic pocket, with heme iron putatively coordinated to two histidine axial ligands. …
• NAID 120005438849

• Purification and properties of a histidine decarboxylase from Staphylococcus epidermidis TYH1 isolated from Japanese fish-miso

• Furutani Ayumi,Harada Yasuyuki,Shozen Kei-ichi [他]
• Fisheries science 80(1), 93-101, 2014-01
• NAID 40019950358

Related Pictures

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★リンクテーブル★

リンク元	「ヒスチジン」
拡張検索	「histidine ammonia-lyase」「L-histidine」「disorders of histidine metabolism」

「ヒスチジン」

　　[★]

英

histidine His H

同

2-アミノ-3-イミダゾールプロピオン酸 2-amino-3-imidazolepropionic acid

関

アミノ酸、アルギニン、リジン

• 極性、塩基性
• 側鎖：

　-CH2-C3H3N2

• イミダゾール(C3H4N2)　＜　プリンの5員環
• アラニンにイミダゾール基が付いたもの

「histidine ammonia-lyase」

　　[★]

ヒスチジンアンモニアリアーゼ

関

histidase

「L-histidine」

　　[★]

L-ヒスチジン

関

histidine

「disorders of histidine metabolism」

　　[★] ヒスチジン代謝異常症