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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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“The enzyme catechol-O-methyltransferase (COMT) is a key component of the DA metabolic pathway (Axelrod and Tomchick 1958) and inhibition of the enzyme has been proposed as a cognitive enhancement strategy (Apud and Weinberger 2007).”
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“The amines were first converted to their 0-methylated analogues by the enzyme COMT, purified from rat liver according to Axelrod & Tomchick (32), in the presence of 3HSAMe.”
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A simple and rapid fluorimetric determination of catechol-O-methyl transferase (COMT) activity
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“Val158Met (Ex4-12 G>A; rs4680) is a common polymorphism that results in a lower activity enzyme.(5) The low-activity Met allele has been positively associated with breast cancer in some, but not all, studies.”
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“As COMT gene codes methylation enzymes metabolizing monoaminergic neurotransmitters, such as dopamine [27], it can also support gender ratio difference.”
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“Although COMT does not methylate most phenols or gallols [23], virtually all catechols are susceptible to methylation including bulkier steroid compounds.”
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“Because CE competitively bind to COMT, the enzyme that decomposes catecholamines (1, 2), it has been speculated that these CE would prevent norepinephrine (NE) from premature decomposition (9).”
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“The Comt gene encodes for catecholamine-O-methyltransferase (COMT), an enzyme responsible for the elimination/inactivation of catecholamines [3].”
BackgroundEvaluation of the Association of COMT Rs4680 Polymorphism with Swimmers’ Competitive Performance
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“Although its role was established in 1958 [12], the COMT enzyme’s function in other pathways and diseases has become an increasingly popular subject of study in recent years.”
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Adrenomedullary Secretion of DOPA, Catecholamines, Catechol Metabolites, and Neuropeptides
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“This is somewhat surprising because the affinity of COMT from rat liver was similar for NE and EPI (Axelrod and Tomchick, 1958; Park, 1986).”
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“…(COMT; EC 2.1.1.6) inactivates a wide variety of a catechol structure-containing molecules in different species from microorganisms to vertebrates by methylating one of the phenolic hydroxyl groups in the substrate (Axelrod and Tomchick, 1958; Guldberg and Marsden, 1975).”
InfluentialIn vitro evaluation of GR69153, a novel catechol-substituted cephalosporin
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“Semisynthetic penicillins with catechol moieties have also been developed (21), some with associated structural modifications to minimize natural, in vivo 0 methylation (1).”
BackgroundMeshi, T., OTSUKA, M., & Satô, Y. (1970) · Biochemical Pharmacology · doi:10.1016/0006-2952(70)90079-1 · Cited by 17
Production of antibodies to catechol-O-methyltransferase (EC 2.1.1.6) of rat liver
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Surtees, R. A. H., & Hyland, Κ. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90252-2 · Cited by 17
A Sensitive Assay for the Determination of Dopamine in Plasma
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Yanokura, M., & Tsukada, K. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91415-2 · Cited by 17
Effects of H2-Antagonists on Androgen Imprinting of Male Hepatic Functions*
Turocy, J. F., Chiang, A., SEELEY, D. H., & Eagon, P. K. (1985) · Endocrinology · doi:10.1210/endo-117-5-1953 · Cited by 17
Comparison of catechol-O-methyltransferase from rat brain, erythrocytes and liver
Bade, P., Christ, W., Rakow, D., & Coper, H. (1976) · Life Sciences · doi:10.1016/0024-3205(76)90115-6 · Cited by 17
NEW METABOLIC CONJUGATES OF STEROIDS
Layne, D. S. (1970) · Elsevier eBooks · doi:10.1016/b978-0-12-257601-0.50008-6 · Cited by 17
Specific tlc, gc, and gc-ms methods for kinetic studies with COMT
Lin, R.-L., & Narasimhachari, N. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90048-7 · Cited by 17
Actions of the thyroid hormones and analogues in vitro on catechol-o-methyltransferase
D'Iorio, A., & Mavrides, C. (1963) · Biochemical Pharmacology · doi:10.1016/0006-2952(63)90199-0 · Cited by 17
Conversion of Natural Substances by Microbial Enzymes
Tamm, C. (1962) · Angewandte Chemie International Edition in English · doi:10.1002/anie.196201781 · Cited by 17
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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