Indirect oxidation of amino acid phenylhydrazides by mushroom tyrosinase

Gąsowska, Beata; Frąckowiak, Bożena; Wojtasek, Hubert

doi:10.1016/j.bbagen.2006.05.001

Cited by 14 publications

(3 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Specifically, complex 4d displayed enzyme activation. Carbonyl hydrazide moiety could form a complex with the active site copper center of tyrosinase enzyme, thus taking an important part in inhibition [17,37,38]. Four out of six Ti(IV) complexes, including 4a, 4e, 4f, and 4h, showed the most potent inhibitors of tyrosinase enzyme in comparison to the standard Kojic acid.…”

Section: Tyrosinase Inhibitory Activitymentioning

confidence: 99%

Synthesis, characterization, lipoxygenase, and tyrosinase inhibitory activities of non- cytotoxic titanium(III) and (IV) hydrazide complexes

Shaikh¹,

Ashiq²,

Jamal³

et al. 2022

Bull. Chem. Soc. Eth.

View full text Add to dashboard Cite

ABSTRACT. Ti(III) and (IV) hydrazide complexes were synthesized, characterized, and screened for their tyrosinase and lipoxygenase inhibitory and cytotoxic activities. The geometry of Ti(III) hydrazide complexes is tentatively assigned as octahedral. Magnetic moments were found around 1.7 B.M. and electronic spectral transition in the range of 495-518 nm. Evaluation of Ti(IV) and Ti(III) hydrazide complexes for tyrosinase and lipoxygenase inhibitory activities revealed varying inhibition potential. Hydrazide ligands were inactive against tyrosinase, while significant activity was observed against lipoxygenase (LOX). Good to moderate inhibition activity was observed by Ti(IV) and Ti(III) hydrazide complexes against both enzymes. At the same time, promising results were obtained for Ti(IV) hydrazide complexes against tyrosinase enzymes suggesting their broad application as tyrosinase inhibitors. Complex 4d possess negative inhibition, thus behaving as a tyrosinase activator. The docking results showed a good correlation between complex experimental activities and binding energies. Cytotoxic investigation revealed the non-toxicity of complexes against normal cells. KEY WORDS: Titanium(III) and titanium(IV) hydrazide complex, Tyrosinase, Lipoxygenase, Inhibition, Molecular docking, Cytotoxicity Bull. Chem. Soc. Ethiop. 2023, 37(2), 315-333. DOI: https://dx.doi.org/10.4314/bcse.v37i2.6

show abstract

Section: Tyrosinase Inhibitory Activitymentioning

confidence: 99%

Synthesis, characterization, lipoxygenase, and tyrosinase inhibitory activities of non- cytotoxic titanium(III) and (IV) hydrazide complexes

Shaikh¹,

Ashiq²,

Jamal³

et al. 2022

Bull. Chem. Soc. Eth.

View full text Add to dashboard Cite

show abstract

“…The melanogenesis process by tyrosinase is essential to protect living organisms from the harmful ultraviolet radiation of sunlight. However, various dermatologic disorders result in the accumulation of excessive levels of epidermal pigments due to the overexpression of tyrosinase . Tyrosinase is also linked to the production of neuromelanin from dopamine in the brain, which may lead to dopamine neurotoxicity and further neurodegeneration .…”

Section: Introductionmentioning

confidence: 99%

“…However, various dermatologic disorders result in the accumulation of excessive levels of epidermal pigments due to the overexpression of tyrosinase. 3 Tyrosinase is also linked to the production of neuromelanin from dopamine in the brain, which may lead to dopamine neurotoxicity and further neurodegeneration. 4 In food chemistry, tyrosinase, known as polyphenol oxidase (PPO), is responsible for the enzymatic reaction that leads to the browning of fruits and vegetables.…”

Section: Introductionmentioning

confidence: 99%

New Class of Tyrosinase Inhibitors, Rotenoids, from Amorpha fruticosa

Moon,

Kim,

Lee

et al. 2023

ACS Omega

View full text Add to dashboard Cite

A series of rotenoids including a new one from the seeds of Amorpha fruticosa were found to have significant potential as tyrosinase inhibitors. All of the isolated rotenoids (1−6) displayed inhibitory activity against tyrosinase, both as a monophenolase for the oxidation of L-tyrosine and as a diphenolase for the oxidation of L-DOPA. The three most active compounds (1, 5, and 6) showed significant monophenolase inhibition with IC 50 values of 2.1, 1.7, and 1.2 μM, respectively. They also inhibited diphenolase function with IC 50 values in the range of 9.5−21.5 μM. The inhibition kinetics established all compounds to be competitive inhibitors of both oxidation processes. All rotenoids formed the E met •I complex effectively around their IC 50 values with long lag times. Tyrosinase inhibition of the new rotenoid 6 was additionally demonstrated using high-performance liquid chromatography (HPLC) analysis with N-acetyl-L-tyrosine. Molecular docking disclosed that the sugar moiety of 5 interacted with the bottom of the catalytic gorge.

show abstract

The Oxidation of Phenylhydrazine by Tyrosinase

Sung

Gayam

2013

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25 °C). The values of k cat and K M for the oxidation of phenylhydrazine were obtained as 11.0 s(-1) and 0.30 mM, respectively. The generation of superoxides during the oxidation of phenylhydrazine by tyrosinase was monitored by nitroblue tetrazolium (NBT) assay. In the phenylhydrazine-tyrosinase reaction, 1 mol O2 was required for the production of 1 mol phenol and 1/6 mol superoxide. The decomposition of superoxide by superoxide dismutase enhanced the rate constant of the oxidation of phenylhydrazine. Phenol formed in the oxidation of phenylhydrazine by tyrosinase was further oxidized by tyrosinase to an o-quinone, after the oxidation of phenylhydrazine by tyrosinase was almost completed.

show abstract

Indirect oxidation of amino acid phenylhydrazides by mushroom tyrosinase

Cited by 14 publications

References 30 publications

Synthesis, characterization, lipoxygenase, and tyrosinase inhibitory activities of non- cytotoxic titanium(III) and (IV) hydrazide complexes

Synthesis, characterization, lipoxygenase, and tyrosinase inhibitory activities of non- cytotoxic titanium(III) and (IV) hydrazide complexes

New Class of Tyrosinase Inhibitors, Rotenoids, from Amorpha fruticosa

The Oxidation of Phenylhydrazine by Tyrosinase

Contact Info

Product

Resources

About