Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Probing enzyme promiscuity of SGNH hydrolases.
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Purified TesA acts mainly as an esterase on p-nitrophenyl esters, with little or no lipase, phospholipase, thioesterase or protease activity.
"TesA, EstA and EstP were shown to function as esterases with different affinities and catalytic efficacies towards p-nitrophenyl butyrate."
Structural and functional characterisation of TesA - a novel lysophospholipase A from Pseudomonas aeruginosa.
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Purified TesA hydrolyses 1-acyl glycerophosphocholines (C6, C12, C16) with high catalytic efficiency, suggesting lysophospholipase A is a physiological activity.
"strongly suggest that lysophospholipase A activity may represent at least one of the physiological functions of TesA"
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TesA is mainly periplasmic in P. aeruginosa.
"These results indicate that TesA is primarily localized in the periplasm."
UniProt entry Q9HZY8 (EST_PSEAE)