Recent Advances in Acyltransferase Domain of Type Ⅰ Polyktide Synthases
- Corresponding author: Li Yongquan, lyq@zju.edu.cn
	            Citation:
	            
		            Shen Jiejie, Mao Xuming, Chen Xin'ai, Li Yongquan. Recent Advances in Acyltransferase Domain of Type Ⅰ Polyktide Synthases[J]. Chinese Journal of Organic Chemistry,
							;2018, 38(9): 2377-2385.
						
							doi:
								10.6023/cjoc201806016
						
					
				
					 
				
	        
 
	                
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The substrates of AT domains are in three forms as carboxylic acid, acyl-CoA and acyl-ACP. Their structures are shown in the form of free carboxylic acid in Figure 3
The data was from protein data bank (PDB, ID: 4AMP). (A) Overall structure of ATDynE8 with malonate. The motifs GHSLG and HAFH in α/β-hydrolase-like core domain were colored red and orange. (B) The catalytic pocket of ATDynE8 domain with malonate. Ser in motif GHSLG and His in motif HAFH, malonate, oxygen and hydrogen atoms were colored green, yellow, red and blue. Hydrogen bonds were shown by the yellow dotted lines