2.7.7.3	malfunction	enzyme inactivation effectively prevents bacterial viability	739482	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the bacteria	-, 737460	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the bacteria, e.g. Escherichia coli strain ARC534, phenotype of enzyme knockout mutant Escherichia coli strain W3110, overview	737460	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the bacteria, e.g. of Haemophilus influenzae strain ATCC 51907	-, 737460	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the bacteria, e.g. of Staphylococcus aureus strain ARC516	-, 737460	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the bacteria, e.g. of Streptococcus pneumoniae strains D39 and ATCC 10813	737460	
2.7.7.3	malfunction	enzyme inhibition causes growth suppression of the cells	737460	
2.7.7.3	metabolism	the enzyme catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway	721197	
2.7.7.3	metabolism	the enzyme catalyzes the penultimate step in coenzyme A biosynthesis	739482	
2.7.7.3	metabolism	the enzyme catalyzes the penultimate step in the coenzyme A biosynthetic pathway	721210	
2.7.7.3	additional information	the enzyme is allosteric in nature and regulated by coenzyme A through feedback inhibition. Structure-function analysis, and analysis of catalytic, allosteric and inhibitory mechanisms involved in regulation of PPAT. Changes in side chains R90 and D94 are responsible for transition between catalytic and allosteric inhibitory states. Diphosphate binds in close vicinity of ATP and produces a 10 A flip in the adenine ring of coenzyme A moiety. Transition of PPAT in Pseudomonas aeruginosa from substrate binding to inhibitory states is triggered by an arginine switch	737781