physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential
enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview
the enzyme catalyzes the last step in each elongation cycle of type II bacterial fatty acid synthesis and is a key regulatory protein in bacterial fatty acid synthesis
the NADH cofactor and the CoA thioester substrate form a covalent adduct during the InhA catalytic cycle. Residue Tyr158 is required for the stereospecificity of protonation and Thr196 is partially involved in hydride transfer and protonation
enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview
the NADH cofactor and the CoA thioester substrate form a covalent adduct during the InhA catalytic cycle. Residue Tyr158 is required for the stereospecificity of protonation and Thr196 is partially involved in hydride transfer and protonation
PfENR reduces the trans-2 enoyl bond of enoyl-ACP substrates to saturated acyl-ACPs and plays a crucial role in completing the successive rounds of fatty acid elongation
expression in Escherichia coli restores growth and the fatty acid synthesis of the Escherichia coli fabl temperature sensitive mutant JP1111 under nonpermissive conditions
fatty acid biosynthesis and FabI activity are essential for growth even in the presence of exogenous long-chain lipids. FabI is not transcriptionally altered in the presence of exogenous long-chain lipids. Inhibition of FabI or fatty acid synthesis results in loss of viability that is not rescued by exogenous long-chain lipid supplementation. FabI and de novo fatty acid biosynthetic genes are transcriptionally active during infection
isoform FabV confers triclosan resistance on Pseudomonas aeruginosa. Upon deletion of the fabV gene, the mutant strain becomes more than 2000fold more sensitive to triclosan than the wild-type strain. Enzyme functionally replaces Escherichia coli fabI in vivo and renders Escherichia coli resistant to triclosan
the enzyme is able to complement an Escherichia coli JP1111 FabI mutant strain. When ENR2 is expressed together with FabI the proportion of saturated fatty acids decreases from 50 to 30%
fatty acid biosynthesis and FabI activity are essential for growth even in the presence of exogenous long-chain lipids. FabI is not transcriptionally altered in the presence of exogenous long-chain lipids. Inhibition of FabI or fatty acid synthesis results in loss of viability that is not rescued by exogenous long-chain lipid supplementation. FabI and de novo fatty acid biosynthetic genes are transcriptionally active during infection