Functional characterization of seven γ-Glutamylpolyamine synthetase genes and the bauRABCD locus for polyamine and β-Alanine utilization in Pseudomonas aeruginosa PAO1.
Functional analysis and regulation of the divergent spuABCDEFGH-spuI operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAO1.
-
spuA mutants are defective in spermidine utilization.
"Although spuA and spuB mutants showed an apparent defect in spermidine utilization, the biochemical functions of the gene products have yet to be elucidated."
Structure and mechanism of the γ-glutamyl-γ-aminobutyrate hydrolase SpuA from Pseudomonas aeruginosa.
-
SpuA prefers gamma-Glu-GABA as substrate in activity and binding assays.
"Activity and substrate-binding assays confirm that SpuA exhibits a preference for γ-Glu-GABA as a substrate."
-
SpuA hydrolyses gamma-Glu-GABA in the gamma-glutamylation putrescine pathway.
"SpuA hydrolyzes γ-glutamyl-γ-aminobutyrate (γ-Glu-GABA) to glutamate and γ-aminobutyric acid (GABA)"
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features