How does chloramphenicol acetyltransferase work?

Bacterial resistance to CAM is caused by the chromosomally or plasmid-encoded enzyme chloramphenicol acetyltransferase (CAT) that catalyzes the transfer of an acetyl group from acetyl-coenzyme A (AcCoA) to the 3-hydroxyl group of CAM [Fig.

What is CAT in plasmid?

Chloramphenicol Acetyltransferase (CAT) Assay* The elements to be tested are fused to the coding region of the bacterial CAT gene present on a recombinant DNA plasmid.

How do bacteria resist chloramphenicol?

The most common mechanism of resistance to chloramphenicol in bacteria is its enzymatic inactivation by acetylation mainly via acetyltransferases or, in some cases, by chloramphenicol phosphotransferases (1, 56).

What is GFP reporter?

Green fluorescent protein is a quantitative reporter of gene expression in individual eukaryotic cells.

Is catalase a gene?

CAT (Catalase) is a Protein Coding gene. Diseases associated with CAT include Acatalasemia and Pityriasis Versicolor. Among its related pathways are Doxorubicin Pathway, Pharmacokinetics and ethanol degradation II.

How do cat genes work?

In each pair of chromosomes, a cat inherited one chromosome from each parent. Therefore, 19 chromosomes are inherited from the mother and 19 from the father. Each chromosome carries distinct variants of genes (alleles). The expression of the genes depends on which alleles the cat carries for each gene.

What is cat antioxidant?

CAT is a common antioxidant enzyme present almost in all living tissues that utilize oxygen. The enzyme uses either iron or manganese as a cofactor and catalyzes the degradation or reduction of hydrogen peroxide (H2O2) to water and molecular oxygen, consequently completing the detoxification process imitated by SOD.

Is chloramphenicol bacteriostatic or bactericidal?

Chloramphenicol is bactericidal at clinically achievable concentrations against Haemophilus influenzae, Streptococcus pneumoniae, and Neisseria meningitidis. It is bacteriostatic against gram-negative bacilli of the family Enterobacteriaceae and against Staphylococcus aureus.

How chloramphenicol inhibits protein synthesis?

Chloramphenicol inhibits microbial protein synthesis by binding to the 50 S subunit of the 70 S ribosome and inhibiting the action of peptidyl transferase, thus preventing peptide bond formation. This mechanism also prevents the binding of aminoacyl transfer RNA to the peptidyl transferase active site.

How does chloramphenicol inhibit bacterial growth?

Chloramphenicol stops bacterial growth by binding to the bacterial ribosome (blocking peptidyl transferase) and inhibiting protein synthesis. Chloramphenicol is lipid-soluble, allowing it to diffuse through the bacterial cell membrane.

Why is GFP important?

Biologists use GFP to study cells in embryos and fetuses during developmental processes. Biologists use GFP as a marker protein. GFP can attach to and mark another protein with fluorescence, enabling scientists to see the presence of the particular protein in an organic structure.

What is cat catalase?

CAT Gene – Catalase Catalase is a heme enzyme that is present in the peroxisome of nearly all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thereby mitigates the toxic effects of hydrogen peroxide.

What is the function of chloramphenicol?

Chloramphenicol is used in the treatment of infections caused by bacteria. It works by killing bacteria or preventing their growth.

How does chloramphenicol stop protein synthesis?

Chloramphenicol inhibits bacterial protein synthesis by binding to the 50S ribosomal subunit. In addition to hematopoietic toxicity, the gray baby syndrome is one of the most notable adverse reactions associated with this agent.

What is the function of transferase?

Transferases participate in a myriad of cell reactions and are also utilized during translation. Mechanistically, an enzyme catalyzing the following reaction would be considered as a transferase: Figure 1. Redox reaction. where X is the donor that is often a coenzyme, and Y is the acceptor.

What is the EC2 classification for transferases?

In the EC numbering system, transferases have been given a classification of EC2. Hydrogen is not considered a functional group when it comes to transferase targets; instead, hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. Reaction involving aspartate transcarbamylase.

What is a transferase reaction?

Mechanistically, an enzyme catalyzing the following reaction would be considered as a transferase: Figure 1. Redox reaction. where X is the donor that is often a coenzyme, and Y is the acceptor. Group would be the functional group that is transferred on account of transferase activity.

What is an example of transferase activity?

Transferase. Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan, and the regulation of pyruvate dehydrogenase (PDH),…