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Enzymatic O-Methylation of Epinephrine and Other Catechols
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“The O-methylation of catechols plays an important role in the phase 2 metabolism of estrogens (Section 4.4.1) and is catalyzed by the enzyme catechol-O-methyltransferase (COMT) [179]”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [179]
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“Considering the fact that there is no evidence for stereospecificity in the activity of par t ia l ly purified COMT (Axelrod and Tomchick 1958), it appears possible that, in our studies, the preferential Omethyla t ion o f ( - ) - i sop rena l i ne was due to a stereoselective entry of isoprenaline into COMT containin…”
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“Catechol-O-methyltransferase, a key enzyme serving the inactivation of dopamine and norepinephrine [1, 2], is encoded by the COMT gene.”
El‐Shorbagi, A., Chaudhary, S., Alshemali Khadeja, A., Alabdulrazzaq Razan, F., & Alqahtani Fatma, Y. (2020) · Journal of Applied Pharmaceutical Science · doi:10.7324/japs.2020.1010015 · Cited by 11
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“Background Catechol-O-methyltransferase (COMT) (MIM 116790) catalyzes the transfer of a methyl group from S-adenosylmethionine to catecholamines [1], and dopamine-betahydroxylase (DBH) (MIM 223360) catalyzes the conversion of dopamine to norepinephrine [2]; both enzymes are involved in the catecholamine metabolism sys…”
Cruz-Vicente, P., Gonçalves, A. M., Ferreira, O., Queiroz, J. A., Silvestre, S., Passarinha, L. A., & Gallardo, E. (2021) · Pharmaceuticals · doi:10.3390/ph15010051 · Cited by 11
“Specifically, COMT is a magnesium-dependent enzyme that mediates the removal of a methyl group from S-adenosyl-L-methionine (SAM) to a catecholic substrate, affording O-methylated products and S-adenosylhomocysteine (AdoHcy) [4].”
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“…biotransformation by transferring a methyl group, and K00274 monoamine oxidase, also known as epinephrine oxidase or serotonin deaminase, responsible for the oxidative deamination of neurotransmitters and biogenic amines, are recognized as key genes in neurotransmitter catabolism 58,59 .”
Manic symptom severity correlates with COMT activity in the striatum: A post-mortem study
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“…dopamine (DA) and norepinephrine (NE) have been extensively implicated in the pathophysiology of schizophrenia and bipolar disorder (BD; Axelrod and Tomchik 1958; van Kammen and Kelley 1991; Manji et al. 2003; Yamamoto and Hornykiewicz 2004; Cousins et al. 2009; Howes and Kapur 2009).”
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“COMT is involved in the inactivation of synaptic dopamine (Axelrod and Tomchick 1958).”
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[37] Enzymes of estrogen metabolism
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“Increases in COMT, an enzyme that contributes to dopamine degradation (Axelrod and Tomchick, 1958, Craddock et al., 2006, Scheggia et al., 2018), could therefore result in less available dopamine via increased dopamine breakdown.”
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“Calcium, magnesium and a series of compounds that inhibit methyltransferase enzymes, at concentrations that are known to be effective in other tissues, were tested for their effects on mouse kidney H N M T activity (Table 1) [22-29].”
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A new synthesis of Entacapone and report on related studies
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Inhibitory Effect of Bovine Lactoferrin on Catechol-O-Methyltransferase
Ikeda, M., Iijima, H., Shinoda, I., Iwamoto, H., & Takeda, Y. (2017) · Molecules · doi:10.3390/molecules22081373 · Cited by 8
“COMT is expressed in various organs, with high activity in the liver and kidneys [23,24].”
Interactions of the enantiomers of 3-O-methyldobutamine with α- and β-adrenoceptors in vitro
Ruffolo, R. R., Jr., Messick, K., & Horng, J. S. (1985) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00501875 · Cited by 8
“1976), was pharmacologically inactive at ~- and ]%adrenoceptors (Leier and Unverferth 1983), as are most catecholamines following O-methylation by catechol-O-methyltransferase (Trendelenburg 1972; Axelrod and Tomchick 1958).”
BackgroundBamshad, J., Serot, D. I., & Szoko, E. W. (1970) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12291779 · Cited by 8
Enzymatic N-O-methylation of hydroxamic acids
Lotlikar, P. D. (1968) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(68)90039-1 · Cited by 8
A 3‐D QSAR Study of Catechol‐O‐Methyltransferase Inhibitors Using CoMFA and CoMSIA
Ai, C., Wang, Y., Li, Y., Li, Y., & Yang, L. (2008) · QSAR & Combinatorial Science · doi:10.1002/qsar.200730053 · Cited by 8
Neuronal expression of catechol O-methyltransferase mRNA in neonatal rat suprachiasmatic nucleus
Shirakawa, T., Abe, M., Oshima, S., Mitome, M., & Oguchi, H. (2004) · Neuroreport · doi:10.1097/01.wnr.0000127635.38052.cd · Cited by 8
“Catechol O-methyltransferase (COMT) is a ubiquitous enzyme involved in the inactivation of catecholamine neurotransmitters [4].”
BackgroundQUESNEY, L. F., & Reader, T. A. (1990) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4684-6767-3_21 · Cited by 8
Metadata
- Authors
- Axelrod, J., & Tomchick, R.
- Affiliations
- United States Public Health Service (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1958-09
- Volume
- 233
- Issue
- 3
- Pages
- 702-705
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1543624067
- Cited by
- 1,283
- References
- 16
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 8 · 2023: 12 · 2022: 14 · 2021: 19 · 2020: 11 · 2019: 16 · 2018: 13 · 2017: 15 · 2016: 28 · 2015: 12 · 2014: 14 · 2013: 19 · 2012: 21
- FWCI
- 55.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Keywords
- epinephrine, catechol, O-methylation, enzymatic methylation, catecholamine metabolism
- MeSH terms
- Catechols, Epinephrine, Methylation, Norepinephrine, Transferases
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