2016Mini-Reviews in Medicinal ChemistryRequires access

Arginine Deiminase Enzyme Evolving as a Potential Antitumor Agent

Rakesh R. Somani, Pratip K. Chaskar

Open publisher page 9 citations

Abstract

Some melanomas and hepatocellular carcinomas have been shown to be auxotrophic for arginine. Arginine deiminase (ADI), an arginine degrading enzyme isolated from Mycoplasma, can inhibit the growth of these tumors. It is a catabolizing enzyme which catabolizes arginine to Citrulline. Tumor cells do not express an enzyme called arginosuccinate synthetase (ASS) and hence, these cells become auxotrophic for arginine. It is found that ADI is specific for arginine and did not degrade other amino acid. This review covers various aspects of ADIs like origin, properties and chemical modifications for better antitumor activity. Keywords: Arginine, Arginine deiminase (ADI), Arginosuccinate synthetase (ASS), Arginosuccinate lyase (ASL), Hepatocellular carcinoma, malignant melanoma.

About this research paper

What this paper is about

Some melanomas and hepatocellular carcinomas have been shown to be auxotrophic for arginine. Arginine deiminase (ADI), an arginine degrading enzyme isolated from Mycoplasma, can inhibit the growth of these tumors. It is a catabolizing enzyme which catabolizes arginine to Citrulline. Tumor cells do not express an enzyme called arginosuccinate synthetase (ASS) and hence, these cells become auxotrophic for arginine. It is found that ADI is specific for arginine and did not degrade other amino acid. This review covers various aspects of ADIs like origin, properties and chemical modifications for better antitumor activity. Keywords: Arginine, Arginine deiminase (ADI), Arginosuccinate synthetase (ASS), Arginosuccinate lyase (ASL), Hepatocellular carcinoma, malignant melanoma.

Why it matters

OpenAlex reports 9 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Some melanomas and hepatocellular carcinomas have been shown to be auxotrophic for arginine. Arginine deiminase (ADI), an arginine degrading enzyme isolated from Mycoplasma, can inhibit the growth of these tumors. It is a catabolizing enzyme which catabolizes arginine to Citrulline. Tumor cells do not express an enzyme called arginosuccinate synthetase (ASS) and hence, these cells become auxotrophic for arginine. It is found that ADI is specific for arginine and did not degrade other amino acid. This review covers various aspects of ADIs like origin, properties and chemical modifications for better antitumor activity. Keywords: Arginine, Arginine deiminase (ADI), Arginosuccinate synthetase (ASS), Arginosuccinate lyase (ASL), Hepatocellular carcinoma, malignant melanoma.

Key concepts: Arginine deiminase, Arginine, Citrulline, Enzyme, Biochemistry, Argininosuccinate synthase, Chemistry, Biology

Related papers

Back to paper searchBrowse research topicsOriginal source
Arginine Deiminase Enzyme Evolving as a Potential Antitumor Agent — Research Paper | ScholarLens