In our lab, a novel enzyme Acetoxcy Drug: Protein Transacetylase (TAase), catalyzing transfer of acetyl group from various polyphenolic peracetate (PA) to certain receptor proteins such as cytochromes P-450, NADPH cytochrome reductase, nitric oxide synthase (NOS) has been established.
Since, a large number of polyphenolic acetates were found to be substrates, the aforementioned enzyme was named Acetoxy drug: protein Transacetylase (TAase).
The earlier work carried out in our laboratory projected PA(s) as irreversible inhibitors of mammalian CYP linked MFO, possibly due to modification of p-450 by way of acetylation catalyzed by acetoxy drug: protein Transacetylase (12-14).
Accordingly, it was hypothesized that the CYP51 of mycobacteria involved in the cell wall sterol synthesis could possibly be modified by our PA(s) through the novel unknown action of GS as transacetylase leading to the death of mycobacterial cells.
Characterization of protein transacetylase from human placenta as a signaling molecule calreticulin using polyphenolic peracetates as the acetyl group donors.
Part 7: Assay and characterization of 7,8-diacetoxy-4-methylcoumarin:protein transacetylase from rat liver microsomes based on the irreversible inhibition of cytosolic glutathione Stransferase.
A new acetyl CoA independent acetylation of proteins catalyzed by acetoxy drug: calreticulin transacetylase system is also described here and its role in modulating the cellular response similar to that of histone deacetylase (HDAC) inhibitors (Fig.
Recent reports describe that transacetylase purified from microsomal bodies of human placenta is identical to calreticulin (73).
Establishment of the enzymatic protein acetylation independent of acetyl CoA: recombinant glutathione S- transferase 3-3 is acetylated by a novel membrane-bound transacetylase using 7, 8-diacetoxy-4-methyl coumarin as the acetyl donor.
Acetoxy drug: protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates.
Calorie restriction promotes mammalian cell survival by inducing the Sirt1 transacetylase.
Sinclair, "Calorie restriction promotes mammalian cell survival by inducing the Sirt1 transacetylase," Science 305, no.