Structural highlights
Function
GNAT2_STRCL Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors.[1]
Publication Abstract from PubMed
Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.
Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.,Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kershaw NJ, McNaughton HJ, Hewitson KS, Hernandez H, Griffin J, Hughes C, Greaves P, Barton B, Robinson CV, Schofield CJ. ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity. Eur J Biochem. 2002 Apr;269(8):2052-9. PMID:11985581
- ↑ Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ. Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates. Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301 doi:10.1039/c1ob05554b
