Interaction of mushroom tyrosinase with aromatic amines, o-diamines and o-aminophenols

Gąsowska, Beata; Kafarski, Paweł; Wojtasek, Hubert

doi:10.1016/j.bbagen.2004.04.013

Cited by 48 publications

(37 citation statements)

References 21 publications

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“…When o-aminophenols, with the exception of 2-amino-4-methylphenol and 3,4-AHBAL, were used as substrates, the products with a phenoxazinone chromophore were followed by measuring the absorbance at 433 nm, characteristic for phenoxazinone derivatives. When 2-amino-4-methylphenol was used as a substrate, the quinone imine produced was dimerized to yield an unknown compound of 14 carbons, but not a phenoxazinone derivative, as determined by 13 C NMR analysis. We did not characterize this compound any further.…”

Section: Accumulation Of 34-ahbal and 34-acahbal In S Griseus Mutantmentioning

confidence: 99%

“…The k cat /K m value for 3,4-dihydroxybenzaldehyde is 25 times smaller than that for 3,4-AHBAL, solely due to the decrease in the k cat value for 3,4-dihydroxybenzaldehyde. Concerning very low rates of aromatic amine and o-aminophenol oxidation by tyrosinases, Gasowska et al (13) pointed out that o-diphenols are deprotonated more readily than arylamines due to a large difference in the pK a value between phenols (pK a ϭ 10) and arylamines (pK a ϭ 27). In addition, GriF had a rather small k cat value (14.0 Ϯ 1.1 s Ϫ1 ) for the best substrate (3,4-AHBAL) compared with that (390 Ϯ 16 s Ϫ1 ) of the tyrosinase for catechol.…”

Section: Grif As a Novel O-aminophenolmentioning

confidence: 99%

“…On the basis of the catalytic properties of tyrosinases and x-ray crystallography of the binuclear copper active sites of hemocyanin (27) and catechol oxidase (28), detailed mechanisms of the tyrosinase reaction as both a monophenolase and a diphenolase have been proposed (29,30). Some tyrosinases seem to have generous substrate specificity; the tyrosinases from N. crassa (12), mushroom (13), and S. glaucescens (12) catalyze the oxidation of aromatic amines, o-diamines, and o-aminophenols, but at a low rate, in addition to phenol and catechol. This study has revealed a unique substrate specificity of GriF, which we can classify as an o-aminophenol oxidase.…”

Section: Grif As a Novel O-aminophenolmentioning

confidence: 99%

“…Tyrosinases are responsible for melanin pigmentation in streptomycetes, browning in plants, and melanization in animals. In addition to the intrinsic tyrosinase activities, the tyrosinases from Neurospora crassa (12), mushroom (13), and Streptomyces glaucescens (12) convert 2-aminophenols into the corresponding o-quinone imines in vitro at a lesser rate, which are then non-enzymatically converted into phenoxazinones.…”

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confidence: 99%

“…2 Because all the biosynthesis and regulatory genes for a certain secondary metabolite are usually contained within the gene cluster, we expected that one of the gene products encoded in this gene cluster is responsible for the formation of the phenoxazinone skeleton of grixazones. Because some tyrosinases show an additional activity to use o-aminophenol as a substrate and yield phenoxazinones (12,13), we aimed at two gene products (GriE and GriF) that are similar to the MelC1 and MelC2 proteins in streptomycetes, respectively. MelC2 is a tyrosinase and MelC1 is a copper chaperon for MelC2.…”

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A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

Suzuki

Furusho

Higashi

et al. 2006

Journal of Biological Chemistry

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Grixazone contains a phenoxazinone chromophore and is a secondary metabolite produced by Streptomyces griseus. In the grixazone biosynthesis gene cluster, griF (encoding a tyrosinase homolog) and griE (encoding a protein similar to copper chaperons for tyrosinases) are encoded. An expression study of GriE and GriF in Escherichia coli showed that GriE activated GriF by transferring copper ions to GriF, as has been observed for a Streptomyces melanogenesis system in which the MelC1 copper chaperon transfers copper ions to MelC2 tyrosinase. In contrast with tyrosinases, GriF showed no monophenolase activity, although it oxidized various o-aminophenols as preferable substrates rather than catechol-type substrates. Deletion of the griEF locus on the chromosome resulted in accumulation of 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) and its acetylated compound, 3-acetylamino-4-hydroxybenzaldehyde. GriF oxidized 3,4-AHBAL to yield an o-quinone imine derivative, which was then non-enzymatically coupled with another molecule of the o-quinone imine to form a phenoxazinone. The coexistence of N-acetylcysteine in the in vitro oxidation of 3,4-AH-BAL by GriF resulted in the formation of grixazone A, suggesting that the -SH group of N-acetylcysteine is conjugated to the o-quinone imine formed from 3,4-AHBAL and that the conjugate is presumably coupled with another molecule of the o-quinone imine. GriF is thus a novel o-aminophenol oxidase that is responsible for the formation of the phenoxazinone chromophore in the grixazone biosynthetic pathway.We have long studied the A-factor regulatory cascade that leads to secondary metabolite formation and morphological differentiation in Streptomyces griseus (1, 2). The A-factor (2-isocapryloyl-3R-hydroxymethyl-␥-butyrolactone) triggers the synthesis of almost all the secondary metabolites produced by this species. One of the secondary metabolites under the control of the A-factor is grixazone. Grixazone is a yellow pigment and actually a mixture of grixazones A and B (compounds 1a and 1b) (see Fig. 2C) (3). Grixazone A is a novel compound, and grixazone B has been reported to show a parasiticide activity (4).Grixazones contain a phenoxazinone chromophore. The phenoxazinone skeleton is common to actinomycin D produced by Streptomyces antibioticus (5), michigazone produced by Streptomyces michiganensis (6), texazone produced by Streptomyces sp. WRAT-210 (7), exfoliazone produced by Streptomyces exfoliatus (8), and 4-demethoxymichigazone produced by Streptomyces halstedii (9). Hsieh and Jones (10) reported a phenoxazinone synthase in S. antibioticus that catalyzes the six-electron oxidative coupling of o-aminophenol compounds derived from tryptophan through 3-hydroxyanthranilic acid. However, disruption of the phenoxazinone synthase gene in S. antibioticus does not affect actinomycin D synthesis, showing that the phenoxazinone skeleton in actinomycin D is biosynthesized in vivo by a still unknown enzyme or non-enzymatically (11). On the other hand, michigazone with a hydroxymethyl group at ...

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Section: Accumulation Of 34-ahbal and 34-acahbal In S Griseus Mutantmentioning

confidence: 99%

Section: Grif As a Novel O-aminophenolmentioning

confidence: 99%

Section: Grif As a Novel O-aminophenolmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

Suzuki

Furusho

Higashi

et al. 2006

Journal of Biological Chemistry

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Free radical generation during the activation of hemolymph prepared from the homopteran Dactylopius coccus

Muñoz

Lanz‐Mendoza

Hernández-Hernández

2007

Arch Insect Biochem Physiol

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Superoxide anion (O(-) (2)) and nitric oxide (NO) generation in Dactylopius coccus hemolymph obtained by perfusion and activated with zymosan was studied. Activated hemolymph reduced 3-[4,5 dimethylthiazolil-2]-2,5-diphenyl tetrazolium bromide. This reduction was prevented by superoxide dismutase (SOD) indicating O(-) (2) generation. This activity was dependent on temperature, and hemolymph incubated at 75 degrees C lost its activity. Chromatocytes incubated with zymosan released their content and produced O(-) (2). Activated hemolymph also produced NO and this activity was prevented in the presence of NG-nitro-L-arginine methyl ester, suggesting that nitric oxide synthase (NOS) might be present in D. coccus hemolymph. The probable source of O(-) (2) in the D. coccus hemolymph is the anthraquinone oxidation, since commercial carminic dye produced O(-) (2) during its oxidation by Agaricus bisporus tyrosinase. Gram+ Micrococcus luteus exposed to activated hemolymph were killed in vitro, and addition of NG-nitro-L-arginine methyl ester and D-Mannitol (a hydroxyl radical scavenger) prevented their killing. The cytotoxic effect produced by the activated hemolymph was not observed with the Gram- bacteria Serratia marcescens. These results suggest that D. coccus activated hemolymph generates reactive oxygen intermediates (ROI) and reactive nitrogen intermediates (RNI) that may limit M. luteus growth.

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Phosphonic and Phosphinic Acid Derivatives as Novel Tyrosinase Inhibitors: Kinetic Studies and Molecular Docking

Wolińska

Hałdys

Góra

et al. 2019

Chemistry & Biodiversity

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A dozen of phosphonic and phosphinic acid derivatives containing pyridine moiety were synthesized and its inhibitory activity toward mushroom tyrosinase was investigated. Moreover, molecular docking of these compounds to the active site of the enzyme was performed. All the compounds (1–10) demonstrated the inhibitory effect with the IC50 and inhibition constants ranging millimolar concentrations. The obtained results indicate that the compounds show different types of inhibition (competitive, noncompetitive, mixed), but all of them are reversible inhibitors. The obtained outcomes allowed to make the structure–activity relationship (SAR) analysis. Compound 4 ([(benzylamino)(pyridin‐2‐yl)methyl]phenylphosphinic acid) revealed the lowest IC50 value of 0.3 mm and inhibitory constant of Ki 0.076 mm, with noncompetitive type and reversible mechanism of inhibition. According to SAR analysis, introducing bulky phenyl moieties to phosphonic and amino groups plays an important role in the inhibitory potency on activity of mushroom tyrosinase and could be useful in design and development of a new class of potent organophosphorus inhibitors of tyrosinase. Combined results of molecular docking and SAR analysis can be helpful in designing novel tyrosinase inhibitors of desired properties. They may have broad application in food industry and cosmetology.

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Interaction of mushroom tyrosinase with aromatic amines, o-diamines and o-aminophenols

Cited by 48 publications

References 21 publications

A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

Free radical generation during the activation of hemolymph prepared from the homopteran Dactylopius coccus

Phosphonic and Phosphinic Acid Derivatives as Novel Tyrosinase Inhibitors: Kinetic Studies and Molecular Docking

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