Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3'-5')-cyclic-GMP in virulence.
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Lysates of a PA3825-overexpressing strain degraded 27% of added c-di-GMP (Table 1, read in PMC full text).
"Analysis of the phenotypes of DGC and PDE mutants and overexpressing clones revealed that certain virulence-associated traits are controlled by multiple DGCs and PDEs through alterations in c-di-GMP levels."
Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases.
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The purified PA3825 EAL domain hydrolyses c-di-GMP to pGpG with a kcat of 0.35 per second in the presence of Mn2+.
"In vitro PA3825EAL was able to convert c-di-GMP to pGpG, with a kcat of 0.35 ± 0.1 s−1, in the presence of Mn2+"
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A PA3825 knockout had no motility phenotype.
"Neither swimming, swarming, nor twitching motilities were affected in the PA3825 knockout strain under conditions tested."
Phenotypic and integrated analysis of a comprehensive Pseudomonas aeruginosa PAO1 library of mutants lacking cyclic-di-GMP-related genes.
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Deletion of PA3825 increases early attachment and flow-cell biofilm biomass.
"deletion of two genes encoding EAL-harboring enzymes, PA2200 and PA3825, resulted in elevated attachment levels, as would be expected for genes encoding PDEs"
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt