Elshafei, Ali M. team published research on Journal of Microbiology, Biotechnology and Food Sciences in 2021 | 144-48-9

144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., Safety of 2-Iodoacetamide

Alkyl iodides react at a faster rate than alkyl fluorides due to the weak C-I bond. Iodo alkanes participate in a variety of organic synthesis reactions, which include the Simmons-Smith reaction (cyclopropanation using iodomethane), 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide. Williamson ether synthesis, Wittig reaction, Grignard reaction, alkyl coupling reactions, and Wurtz reaction. Safety of 2-Iodoacetamide.

Elshafei, Ali M.;El-Ghonemy, Dina H. research published 《 Extracellular glutaminase-free L-asparaginase from Trichoderma viride F2: purification, biochemical characterization and evaluation of its potential in mitigating acrylamide formation in starchy fried food》, the research content is summarized as follows. L-asparaginase is an antitumor agent that suppresses cancer cell growth by eliminating L-asparagine from malignant cells. However, the intrinsic glutaminase activity is responsible for significant life-threatening adverse effects. Therefore, glutaminase-free L-asparaginase is far required to improve the therapeutic efficacy of L-asparaginase treatment. L-asparaginase was also used to combat the development of acrylamide in foods rich in carbohydrates cooked at high temperatures Therefore, this study explores the purification and characterization of glutaminase-free L-asparaginase from Trichoderma viride F2 using agro-industrial residues as substrate. The enzyme was purified 36-folds with 688.1 U/mg specific activity and a final yield of 38.9% through ethanol precipitation, gel filtration on Sephadex G-100 followed by Sephadex G-200. The purified L-asparaginase is monomeric with a mol. mass of 57 kDa and exhibited optimum activity at pH 7.5 and 37 °C, which is relatively close to the human body′s internal environment. The purified L-asparaginase showed high affinity and catalytic efficiency towards its natural substrate L-asparagine with Km and Vmax of 1.2 mM and 71.3 U/mL, resp., and did not exhibit any intrinsic glutaminase activity. Among the salts tested, the univalent cations Na+ and K+ enhanced the activity by 145.7% and 163.5%, resp., while the presence of Ag+ and Fe+3 displayed a considerable loss in activity. The enzyme showed a good anti-oxidant activity with IC50 of 66.1μg/mL and was able to convert L-asparagine exist in potatoes to L-aspartic acid and ammonia, suggesting its use as anti-carcinogenic agent and as potential food industry candidate to mitigate acrylamide content in starchy fried food.

144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., Safety of 2-Iodoacetamide

Referemce:
Iodide – Wikipedia,
Iodide – an overview | ScienceDirect Topics – ScienceDirect.com