EC Number   |
General Information |
Reference  |
|---|
    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 the coenzyme A biosynthetic pathway |
721210 |
| 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 | more |
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 |
| 2.7.7.3 | malfunction |
enzyme inactivation effectively prevents bacterial viability |
739482 |
