Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.
The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-epimerase activity, is needed for alginate polymer formation.
-
P. fluorescens AlgG deletion versus inactive variants separates polymer protection from epimerization. Abstract access.
"AlgL, whose in vivo activity is much more limited in the presence of AlgG"
Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG.
-
P. syringae AlgG structure and enzyme mutants; supports conserved polymer epimerization, not target-specific residues or block distribution.
"the structure of Pseudomonas syringae AlgG has been determined"
Falcon deep research fallback report for algG
The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa.
Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product.
-
P. aeruginosa purified AlgG kinetics and NMR product analysis demonstrate that contiguous G residues can form in vitro; physiological Pseudomonas polymer composition is not an absolute catalytic restriction. Abstract access.
"tracts of adjacent guluronate residues were readily formed"
Chemical mechanism and specificity of the C5-mannuronan epimerase reaction.
-
P. aeruginosa mechanistic assays report no bias for neighboring M versus G and irreversibility under the tested conditions. Abstract access.
"the enzyme showed no bias for mannuronate residues adjacent to guluronates versus those adjacent to mannuronates"
Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan epimerase.
-
Recombinant P. aeruginosa AlgG converts polymer mannuronate to guluronate; this is donor chemistry for the KT2440 inference.
"Epimerization was also detected in the in vitro reaction between recombinant AlgG and poly-D-mannuronate, using high-performance anion-exchange chromatography."