6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	catalytic regions analysis	-, 664193	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	molecular surface of the active site of the carboxyltransferase domain	666936	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	non-ordered ter ter mechanism	37629	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	ordered bi bi uni uni ping-pong mechanism	37586	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	ordered mechanism	37608	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	substrate specificity, catalytic mechanism, and structural features	661098	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	the enzyme is bifunctional exhibiting both acetyl-CoA carboxylase and propionyl-CoA carboxylase, EC 6.4.1.3, activities	-, 662786	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	the enzyme proceeds through a hybrid (two-site) random Ter Ter mechanism, one that likely involves a two-step reaction at the biotin carboxylase domain	702459	
6.4.1.2	ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA	two-step reaction mechanism, structure-activity relationship	664564