4-Hydroxyphenylacetaldehyde

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Contents

4-Hydroxyphenylacetaldehyde
4-hydroxyphenylacetaldehyde.svg
Names
Preferred IUPAC name
(4-Hydroxyphenyl)acetaldehyde
Other names
p-Hydroxyphenylacetaldehyde
Identifiers
3D model (JSmol)
3DMet
ChEBI
ChemSpider
ECHA InfoCard 100.216.847 OOjs UI icon edit-ltr-progressive.svg
EC Number
  • 689-849-1
KEGG
PubChem CID
UNII
  • InChI=1S/C8H8O2/c9-6-5-7-1-3-8(10)4-2-7/h1-4,6,10H,5H2
    Key: IPRPPFIAVHPVJH-UHFFFAOYSA-N
  • C1=CC(=CC=C1CC=O)O
Properties
C8H8O2
Molar mass 136.150 g·mol−1
AppearanceWhite solid
Melting point 118 °C (244 °F; 391 K)
Hazards
GHS labelling:
GHS-pictogram-exclam.svg
Warning
H302, H312, H315, H319, H332, H335
P261, P264, P270, P271, P280, P301+P312, P302+P352, P304+P312, P304+P340, P305+P351+P338, P312, P321, P322, P330, P332+P313, P337+P313, P362, P363, P403+P233, P405, P501
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

4-Hydroxyphenylacetaldehyde, also known as p-hydroxyphenylacetaldehyde, is a natural product with the formula HOC6H4CH2CHO. It is a derivative of phenylacetaldehyde and occurs as a white solid at room temperature. [1]

Synthesis

4-Hydroxyphenylacetaldehyde can be synthesized from a parsley tyrosine decarboxylase (L-tyrosine). [2]

Occurrence

4-Hydroxyphenylacetaldehyde is produced from the metabolism of tyramine by monoamine oxidase (MAO) enzymes in humans and the tyramine oxidase (tynA) enzyme in Escherichia coli . [3] [4] In both species, it is subsequently metabolized into 4-hydroxyphenylacetate by aldehyde dehydrogenase (ALDH) enzymes in humans and the phenylacetaldehyde dehydrogenase (feaB) enzyme in E. coli. [3] [4] [5]

The condensation of 4-hydroxyphenylacetaldehyde and dopamine is a key step in the biosynthesis of benzylisoquinoline alkaloids. These natural products include berberine and morphine. [6]

Related Research Articles

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<span class="mw-page-title-main">Phenethylamine</span> Organic compound, a stimulant in humans

Phenethylamine (PEA) is an organic compound, natural monoamine alkaloid, and trace amine, which acts as a central nervous system stimulant in humans. In the brain, phenethylamine regulates monoamine neurotransmission by binding to trace amine-associated receptor 1 (TAAR1) and inhibiting vesicular monoamine transporter 2 (VMAT2) in monoamine neurons. To a lesser extent, it also acts as a neurotransmitter in the human central nervous system. In mammals, phenethylamine is produced from the amino acid L-phenylalanine by the enzyme aromatic L-amino acid decarboxylase via enzymatic decarboxylation. In addition to its presence in mammals, phenethylamine is found in many other organisms and foods, such as chocolate, especially after microbial fermentation.

<span class="mw-page-title-main">Tyramine</span> Chemical compound

Tyramine, also known under several other names, is a naturally occurring trace amine derived from the amino acid tyrosine. Tyramine acts as a catecholamine releasing agent. Notably, it is unable to cross the blood-brain barrier, resulting in only non-psychoactive peripheral sympathomimetic effects following ingestion. A hypertensive crisis can result, however, from ingestion of tyramine-rich foods in conjunction with the use of monoamine oxidase inhibitors (MAOIs).

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<span class="mw-page-title-main">Noscapine</span> Chemical compound

Noscapine is a benzylisoquinoline alkaloid, of the phthalideisoquinoline structural subgroup, which has been isolated from numerous species of the family Papaveraceae. It lacks significant hypnotic, euphoric, or analgesic effects affording it with very low addictive potential. This agent is primarily used for its antitussive (cough-suppressing) effects.

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<span class="mw-page-title-main">Chorismic acid</span> Chemical compound

Chorismic acid, more commonly known as its anionic form chorismate, is an important biochemical intermediate in plants and microorganisms. It is a precursor for:

<span class="mw-page-title-main">Apigenin</span> Chemical compound

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<span class="mw-page-title-main">Amino acid synthesis</span> The set of biochemical processes by which amino acids are produced

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).

<span class="mw-page-title-main">Shikimate dehydrogenase</span> Enzyme involved in amino acid biosynthesis

In enzymology, a shikimate dehydrogenase (EC 1.1.1.25) is an enzyme that catalyzes the chemical reaction

In enzymology, an erythrose-4-phosphate dehydrogenase (EC 1.2.1.72) is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Higenamine</span> Chemical compound

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<span class="mw-page-title-main">Benzylisoquinoline</span> Chemical compound

Substitution of the heterocycle isoquinoline at the C1 position by a benzyl group provides 1‑benzylisoquinoline, the most widely examined of the numerous benzylisoquinoline structural isomers. The 1-benzylisoquinoline moiety can be identified within numerous compounds of pharmaceutical interest, such as moxaverine; but most notably it is found within the structures of a wide variety of plant natural products, collectively referred to as benzylisoquinoline alkaloids. This class is exemplified in part by the following compounds: papaverine, noscapine, codeine, morphine, apomorphine, berberine, tubocurarine.

Molybdopterin synthase (EC 2.8.1.12, MPT synthase) is an enzyme required to synthesize molybdopterin (MPT) from precursor Z (now known as cyclic pyranopterin monophosphate). Molydopterin is subsequently complexed with molybdenum to form molybdenum cofactor (MoCo). MPT synthase catalyses the following chemical reaction:

<i>meta</i>-Tyramine Chemical compound

meta-Tyramine, also known as m-tyramine and 3-tyramine, is an endogenous trace amine neuromodulator and a structural analog of phenethylamine. It is a positional isomer of para-tyramine, and similarly to it, has effects on the adrenergic and dopaminergic systems.

<span class="mw-page-title-main">2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase</span> Enzyme

In enzymology, SEPHCHC synthase (EC EC 2.2.1.9), encoded by menD gene in E. coli, is an enzyme that catalyzes the second step of menaquinone (vitamin K2) biosynthesis. The two substrates of this enzyme are 2-oxoglutarate and isochorismate. The products of this enzyme are 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate and CO2. It belongs to the transferase family.

References

  1. "4-Hydroxyphenylacetaldehyde". PubChem Compound. U.S. National Library of Medicine: National Center for Biotechnology Information. 3 August 2019. Retrieved 8 August 2019. (4-hydroxyphenyl)acetaldehyde is an alpha-CH2-containing aldehyde and a member of phenylacetaldehydes. It has a role as a human metabolite, an Escherichia coli metabolite and a mouse metabolite.
  2. Torrens-Spence, Michael P.; Gillaspy, Glenda; Zhao, Bingyu; Harich, Kim; White, Robert H.; Li, Jianyong (11 February 2012). "Biochemical evaluation of a parsley tyrosine decarboxylase results in a novel 4-hydroxyphenylacetaldehyde synthase enzyme". Biochemical and Biophysical Research Communications. 418 (2): 211–216. doi:10.1016/j.bbrc.2011.12.124. PMID   22266321.
  3. 1 2 "4-Hydroxyphenylacetaldehyde". Human Metabolome Database – Version 4.0. University of Alberta. 23 July 2019. Retrieved 8 August 2019.
  4. 1 2 Elovaara H, Huusko T, Maksimow M, Elima K, Yegutkin GG, Skurnik M, Dobrindt U, Siitonen A, McPherson MJ, Salmi M, Jalkanen S (2015). "Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate". PLOS ONE. 10 (11): e0142367. Bibcode:2015PLoSO..1042367E. doi: 10.1371/journal.pone.0142367 . PMC   4640556 . PMID   26556595.
  5. Universal protein resource accession number P80668 at UniProt.
  6. Samanani N, Liscombe DK, Facchini PJ (2004). "Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis". Plant Journal. 40 (2): 302–313. doi:10.1111/j.1365-313X.2004.02210.x. PMID   15447655.