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UniProt functional annotation for P00805 | ||
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| UniProt code: P00805. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Catalytic activity: | |
Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000269|PubMed:8706862}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.115 uM for L-asparagine; |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:4561256, ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862}. |
| Subcellular location: | |
Periplasm. |
| Induction: | |
By cAMP and anaerobiosis. |
| Pharmaceutical: | |
Available under the names Crastinin (Bayer), Elspar (Merck), Kidrolase (Rhone-Poulenc) and Leunase (Kyowa). Also available as a PEG-conjugated form (Pegaspargase) under the name Oncaspar (Enzon). Used as an antineoplastic in chemotherapy. Reduces the quantity of asparagine available to cancer cells. |
| Miscellaneous: | |
E.coli contains two L-asparaginase isoenzymes: L- asparaginase I, a low-affinity enzyme located in the cytoplasm, and L- asparaginase II, a high-affinity secreted enzyme. |
| Similarity: | |
Belongs to the asparaginase 1 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.