6.2.1.30	evolution	PaaK1 and PaaK2 form a unique subgroup within the adenylate-forming enzyme superfamily	-, 727874	
6.2.1.30	metabolism	PCL is essentially involved in the pathway of penicillin biosynthesis, overview. Conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental to antibiotic production	-, 713830	
6.2.1.30	metabolism	the enzyme catalyzes the second last step in penicillin N biosynthesis in microbodies, pathway overview and interorganelle intermediate transport	716117	
6.2.1.30	additional information	adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview	-, 727874	
6.2.1.30	additional information	conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production	-, 713830	
6.2.1.30	additional information	conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental for antibiotic production. The number of peroxisomes in a dnm1 overexpression strain variant is enhanced relative to those of wild-type controls	-, 713830	
6.2.1.30	additional information	insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2	-, 727575	
6.2.1.30	additional information	insertional mutagenesis of paaK1, which encodes phenylacetate-CoA ligase, does not result in a phenylacetate-conditional growth probably due to the presence of a putative paralogue gene paaK2. The paaK1 deletion mutant IAI1 does not show any growth-defective phenotype in phenylacetate	-, 727575	
6.2.1.30	additional information	isozyme PaaK1 shows dynamic enzyme-substrate interactions. Adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 occur in distinct conformations, a N-terminal microdomain may serve to recruit subsequent phenylacetate enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2, an extended aryl binding pocket in PaaK1 contrasts with PaaK2, overview	-, 727874	
6.2.1.30	physiological function	in a mutant lacking a 6-phophogluconate dehydratase and therefore unable to produce 2-keto-3-deoxy-6-phosphogluconate, phenylacetyl-CoA ligase activity is high, even in the presence of glucose plus phenylacetic acid. In wild-type, phenylacetyl-CoA ligase activity is low under these conditions	-, 705560