The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
the ICL family includes five subfamilies, and the 2-methylisocitrate lyase (MICL) family. The ICL from Pseudomonas aeruginosa (ICL-Pa) is identified in a different ICL node (subfamily 3) than other Pseudomonas ICL enzymes, phylogenetic analysis
the enzyme regulates the type III secretion system, T3SS, overview. Expression of the T3SS in oxygen-limited growth conditions is strongly dependent on the glyoxylate shunt enzyme, isocitrate lyase, which probably affects the RetS/LadS signalling pathways. ICL-dependent regulation of the T3SS does not alter the expression level of the master transcriptional regulator, ExsA, but affects expression of the T3 structural proteins, effectors and regulators, ExsC, ExsD and ExsE
an aceA mutant displays enhanced biofilm formation during anaerobic growth. Expression of PcrV, of PopN (a regulator of the T3SS translocation process), ExoS (a T3 effector protein), and ExsD (a T3S regulator) is greatly reduced in the aceA mutant. Expression of aceA from a plasmid in trans can restore PcrV expression and ICL activity in the aceA mutant
the enzyme is important in the glyoxylate shunt pathway, which is strongly induced in Pseudomonas aeruginosa during anaerobic growth and during growth on C2-sources, such as acetate or fatty acids, as the sole carbon source, overview
conserved residues in the subfamily 3 signature of ICL-Pa play important roles in catalysis and thermostability and are likely associated with the catalytic loop structural conformation. Three-dimensional structural homology modeling of ICL-Pa wild-type and mutants, structure comparisons, active site modeling, overview. Residue N214 plays an essential role in ICL-Pa catalytic activity
conserved residues in the subfamily 3 signature of ICL-Pa play important roles in catalysis and thermostability and are likely associated with the catalytic loop structural conformation. Three-dimensional structural homology modeling of ICL-Pa wild-type and mutants, structure comparisons, active site modeling, overview. Residue N214 plays an essential role in ICL-Pa catalytic activity
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows 10fold reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
Residues Asn214, Gln211, Glu219 and Gln221 contained in the subfamily 3 catalytic signature of the isocitrate lyase from Pseudomonas aeruginosa are involved in its catalytic and thermal properties