The hydroxylation of phenylalanine and tyrosine: A comparison with salicylate and tryptophan

Maskos, Zofia; Rush, J. D.; Koppenol, Willem H.

doi:10.1016/0003-9861(92)90606-w

Cited by 115 publications

(73 citation statements)

References 41 publications

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“…Phenylalanine residues are oxidized to ortho-and meta-tyrosine derivatives [72][73][74]. Tyrosine residues may also react with hydrogen peroxide, yielding 3,4-dihydroxy (dopa) derivative [72,75,76], or bi-tyrosine cross-linked derivatives [73,[77][78][79].…”

Section: Inactivation Of Enzymes By Modification With Hydrogen Peroxidementioning

confidence: 99%

“…Tyrosine residues may also react with hydrogen peroxide, yielding 3,4-dihydroxy (dopa) derivative [72,75,76], or bi-tyrosine cross-linked derivatives [73,[77][78][79]. Tryptophan residues are converted to the 2-, 4-, 5-, 6-, or 7-hydroxy derivatives, and also to N-formylkynurenine and kynurenine [72,[80][81][82].…”

Section: Inactivation Of Enzymes By Modification With Hydrogen Peroxidementioning

confidence: 99%

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Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

140

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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Section: Inactivation Of Enzymes By Modification With Hydrogen Peroxidementioning

confidence: 99%

Section: Inactivation Of Enzymes By Modification With Hydrogen Peroxidementioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

140

107

View full text Add to dashboard Cite

show abstract

“…• OH reacts with L-Phe primarily yielding 2-hydroxy(o-tyrosine), 3-hydroxy(m-tyrosine), and 4-hydroxyphenylalanine ( p-tyrosine), which can be separated by HPLC (22,23). In fact, HPLC measurement of transcardiac tyrosine formation after infusing L-Phe has been used to detect…”

mentioning

confidence: 99%

Detection of Hydroxyl Radicals by -Phenylalanine Hydroxylation: A Specific Assay for Hydroxyl Radical Generation in Biological Systems

Biondi

Xia²,

Rossi

et al. 2001

Analytical Biochemistry

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“…Moreover cells contain thioredoxin reductases that catalyze the NADPH-dependent reduction of oxidized thioredoxin [Th(SS)] back to Th(SH) 2 (reaction 3). Accordingly the coupling of reactions (1), (2), and (3) is described by reaction (4), and coupling provides a biological mechanism Garrison, 1987;Swallow, 1960;Brodie and Reed, 1990;Takahashi and Goto, 1990;Zhou and Gafni, 1991 Garrison et al, 1962;Pryor et al, 1994;Vogt, 1995;, 1998 Phenylalanine 2-, 3-, and 4-Hydroxyphenylalanine; 2,3-dihydroxyphenylalanine Fletcher and Okada, 1961;Solar, 1985;Maskos et al, 1992a, b;Beckman et al, 1992;Gieseg et al, 1993 Proline Glutamylsemialdehyde; 2-pyrrolidone, 4-and 5-OH-proline; pyroglutamic acid Creeth et al, 1983;Poston, 1988;Amici et al, 1989;Uchida et al, 1990;Kato et al, 1992 Tryptophan 2-, 4-, 5-, 6-, 7-Hydroxytryptophan; formylkynurenine; 3-OH-kynurenine; nitrotryptophan Armstrong and Swallow, 1969;Winchester and Lynn, 1970;Maskos et al, 1992a;Guptasarma et al, 1992;Pryor and Uppu, 1993;Kikugawa et al, 1994 Tyrosine 3,4-Dihydroxyphenylalanine; tyr-tyr cross-links; 3-nitrotyrosine; 3-chlorotyrosine; 3,5-dichlorotyrosine Fletcher and Okada, 1961;Maskos et al, 1992a;Beckman et al, 1992;Giulivi and Davies, 1993;Heinecke et al, 1993;Dean et al, 1993;Huggins et al, 1993, van der Vliet et al, 1995…”

Section: Methionine Oxidationmentioning

confidence: 97%