Gene Ontology annotation through association of InterPro records with GO terms
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
Combined Automated Annotation using Multiple IEA Methods
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts.
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AnsB is the active periplasmic asparaginase II.
"Most of the active recombinant enzyme can be released from the
periplasmic space"
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AnsB is exported into the bacterial periplasm.
"Most of the active recombinant enzyme can be released from the
periplasmic space"
Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains.
Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site.
Refolding and purification of recombinant L-asparaginase from inclusion bodies of E. coli into active tetrameric protein.
Localization of the two-L-asparaginases in anaerobically grown Escherichia coli.
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins.
ansB curated UniProt record
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AnsB is the active periplasmic asparaginase II.
"Reaction=L-asparagine + H2O = L-aspartate + NH4(+);"
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Specify L-asparagine breakdown.
"Reaction=L-asparagine + H2O = L-aspartate + NH4(+);"
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AnsB directly catalyzes asparagine catabolism.
"Reaction=L-asparagine + H2O = L-aspartate + NH4(+);"