<i>In vitro</i>effect of novel β-lactam compounds on xanthine oxidase enzyme activity

Bytyqi-Damoni, Arlinda; Genc, Hayriye; Zengin, Mustafa; Beyaztaş, Serap; Gençer, Nahit; Arslan, Oktay

doi:10.3109/10731199.2012.678943

Cited by 19 publications

(15 citation statements)

References 31 publications

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“…The XO inhibitory effect of the cerium vanadate compounds was found to be 0.14-0.2 mM range as listed in Table 1. As you can see from the results, the new cerium vanadate compounds also showed a powerful inhibition when we compare other results in the literature 33 . Furthermore, the standard inhibitor of XO (allopurinol) had an IC 50 value of 7.4 (±0.07) mM was given in the literature 34 .…”

Section: Resultsmentioning

confidence: 62%

Differentialin vitroinhibition studies of some cerium vanadate derivatives on xanthine oxidase

Kaya

Çelik

et al. 2014

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this preliminary study, a new series of some cerium vanadate derivatives have been investigated as new type of inhibitors of xanthine oxidase (XO; E.C 1.17.3.2). XO is a superoxideproducing enzyme found normally in serum and the lungs, and its activity is concerned with several important health problems such as gout, severe liver damage, vascular dysfunction and injury, oxidative eye injury and renal failure. In this study, we present a critical overview of the effects of these novel type agents on XO with comparing the efficacy and safety profiles of allopurinol, the efficient classical inhibitor of XO.

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Section: Resultsmentioning

confidence: 62%

Differentialin vitroinhibition studies of some cerium vanadate derivatives on xanthine oxidase

Kaya

Çelik

et al. 2014

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…These compounds inhibited XO with IC 50 values ranging from 21.65 to 58.04 μM. The most effective compound was 4‐(4‐chlorophenyl)‐1‐(9‐ethyl‐9H‐carbazol‐3‐yl)‐3‐phenylazetidin‐2‐one having an IC 50 of 21.65 μM . In 2013, Lien et al.…”

Section: Xanthine Oxidasementioning

confidence: 99%

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

Kumar

Joshi

Kler

et al. 2017

Medicinal Research Reviews

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Almost all drug molecules become the substrates for oxidoreductase enzymes, get metabolized into more hydrophilic products and eliminated from the body. These metabolites sometime may be more potent, active, inactive, or toxic in nature compared to parent molecule. Xanthine oxidoreductase and aldehyde oxidase belong to molybdenum containing family and are well characterized for their structures and functions, in particular to their ability to oxidize/hydroxylate the xenobiotics. Their upregulated clinical levels causing oxidative stress are associated with pathways either directly involved in the progression of diseases, gout, or indirectly with the succession of other diseases such as diabetes, cancer, etc. Herein, we have put forth a comprehensive review on the xanthine and aldehyde oxidases pertaining to their structures, functions, pathophysiological role, and a comparative analysis of structural insights of xanthine and aldehyde oxidases' binding domains with endogenous ligands or inhibitors. Though both the enzymes are molybdenum containing and are likely to share some common pathways and interact with inhibitors in a similar manner but we have focused on structural prerequisites for inhibitor specificity to both the enzymes keeping in view of the existing X-ray structures. This review also provides futuristic implications in the design of inhibitors derived from inorganic complexes or small organic molecules considering the spatial features and structural insights of both the enzymes.

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“…In our previous studies, it has been proven that β-lactam compounds can also be used as an enzyme inhibitor or activator. [10,18,19,20] From this point of view, we thought that the PPO enzyme assigned in phenol oxidation may be affected by the presence of β-lactam, which is sensitive to reducers. [21,22] On the other hand, the carbazole structure located in the other part of the lactam bearing molecule is a valuable side group for a potential drug because of found in many natural products and drugs.…”

Section: Introductionmentioning

confidence: 99%

Novel β‐Lactam Compounds as Activators for Polyphenoloxidase

Bytyqi-Damoni¹,

Genc

Zengin

et al. 2020

ChemistrySelect

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A copper-containing enzyme polyphenol oxidase (other name is tyrosinase) plays crucial role in melanin biosynthesis, as a compound responsible for human pigmentation. Non controlled loss of melanin can cause hypopigmentation disease. The hypopigmentatory disorder can be treated with melanogenesis stimulators. Here, twenty-four new β-lactam compounds were synthesized, characterized and in vitro effects of them on banana tyrosinase investigated. The enzyme has been purified from banana by an affinity gel comprised of Sepharose4BÀ L-tyrosine-p-aminobenzoic acid. The results showed that the compounds have an effect on increasing the activity of tyrosinase enzyme. Molecules having a notable tyrosinase activator effects are compound 3 h (79.86) and compound 4 n (61.30). The maximal activation, 131% was determined at 130 μM concentration. These results suggested that compounds 3 h and 4 n might represent a novel approach for an effective therapy for diseases associate with tyrosinase dysfunction, such as vitiligo and hair graying.

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In vitroeffect of novel β-lactam compounds on xanthine oxidase enzyme activity

Cited by 19 publications

References 31 publications

Differentialin vitroinhibition studies of some cerium vanadate derivatives on xanthine oxidase

Differentialin vitroinhibition studies of some cerium vanadate derivatives on xanthine oxidase

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

Novel β‐Lactam Compounds as Activators for Polyphenoloxidase

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