Functional analysis and regulation of the divergent spuABCDEFGH-spuI operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAO1.
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Spermidine uptake is greatly reduced in spuD and spuE mutants.
"Second, spermidine uptake is inducible in spermidine-grown cells and is greatly reduced in either spuD or spuE mutant (Fig."
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The authors concluded that SpuD and SpuE prefer spermidine as transport ligand.
"Contrary to such sequence similarities, SpuD and SpuE prefer spermidine rather than putrescine as the transport ligand as determined empirically in this report."
Structural basis of substrate binding specificity revealed by the crystal structures of polyamine receptors SpuD and SpuE from Pseudomonas aeruginosa.
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SpuD is a putrescine-preferential binding protein; SpuE binds only spermidine.
"we found that SpuD is a putrescine-preferential binding protein, while SpuE binds to spermidine exclusively."
UniProt entry Q9I6J1
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SpuD binds putrescine with high affinity and spermidine with low affinity.
"Binds putrescine with high affinity (KD=3 nM), spermidine with relatively low affinity (KD=6.8 uM)."
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods