Establishment of the enzymatic protein acetylation independent of acetyl CoA: recombinant glutathioneS-transferase 3-3 is acetylated by a novel membrane-bound transacetylase using 7,8-diacetoxy-4-methyl coumarin as the acetyl donor-Reference-Cited by-同舟云学术

Establishment of the enzymatic protein acetylation independent of acetyl CoA: recombinant glutathioneS-transferase 3-3 is acetylated by a novel membrane-bound transacetylase using 7,8-diacetoxy-4-methyl coumarin as the acetyl donor

Published:2002-09-28 Issue:1-3 Volume:530 Page:139-142
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Kohli Ekta,Gaspari Marco,Raj Hanumantharao G,Parmar Virinder S,van der Greef Jan,Gupta Garima,Kumari Ranju,Prasad Ashok K,Goel Sanjay,Pal Giridhari,Tyagi Yogesh K,Jain Subhash C,Ahmad Nizamuddin,Watterson Arthur C,Olsen Carl E

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference15 articles.

1. A novel CoA-independent transacetylase produces the ethanolamine plasmalogen and acyl analogs of platelet-activating factor (PAF) with PAF as the acetate donor in HL-60 cells.

2. Purification and Characterization from Rat Kidney Membranes of a Novel Platelet-activating Factor (PAF)-dependent Transacetylase That Catalyzes the Hydrolysis of PAF, Formation of PAF Analogs, and C2-ceramide

3. The enzymatic transacetylation between aromatic amines

4. Histone acetyltransferases: Preparation of substrates and assay procedures

5. Inhibition of Prostaglandin Synthesis as a Mechanism of Action for Aspirin-like Drugs

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