http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID199205
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Bacterial L-asparaginases and related enzymes. Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase. |
| title | L-asparaginase_like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20703599 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8413862 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9989667 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30687441 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16541850 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/31598746 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8477329 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10366895 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29292293 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19367216 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 18.