EC Number   |
Application |
Reference |
|---|
    4.3.2.1 | analysis |
the rapid and sensitive assay method is used to detect increases in the activity in serum from patients with liver diseases |
34420 |
| 4.3.2.1 | diagnostics |
the enzyme may be used as a candidate marker for serodiagnosis of brucellosis |
-, 730344 |
| 4.3.2.1 | diagnostics |
the urea cycle metabolite argininosuccinate is a common metabolic biomarker of FH deficiency |
729518 |
| 4.3.2.1 | drug development |
argininosuccinate lyase (ASL) is overexpressed in breast cancer and downregulation of argininosuccinate lyase decreases tumor growth by inhibiting cyclin A2 and NO. Administration of ASL shRNA may be a treatment to prevent cancer cell proliferation and induce cancer cell death |
748794 |
| 4.3.2.1 | medicine |
argininosuccinate lyase (ASL) is overexpressed in breast cancer and downregulation of argininosuccinate lyase decreases tumor growth by inhibiting cyclin A2 and NO. Administration of ASL shRNA may be a treatment to prevent cancer cell proliferation and induce cancer cell death |
748794 |
| 4.3.2.1 | medicine |
argininosuccinate lyase is a valuable marker for estimating hepatopathy |
699183 |
| 4.3.2.1 | medicine |
argininosuccinate lyase is present in activated microglia cells in the ischemic rat |
679695 |
| 4.3.2.1 | medicine |
expression of mutant ASL proteins in Escherichia coli. The known classical p.Q286R, the novel classical p.K315E and the known mutations p.I100T, p.E189G and p.R385C, which all have been linked to a mild phenotype of argininosuccinic aciduria, show no significant residual activity. There is some enzyme activity detected with the p.V178M (5% of wild-type), and p.R379C (10% of wild-type) mutations in which Km values for argininosuccinic acid differs significantly from the wild-type ASL protein |
715811 |
| 4.3.2.1 | medicine |
loss of function of fumarate hydratase, the mitochondrial tumor suppressor and tricarboxylic acid cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer The accumulation of fumarate leads to reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells from Fh1-deficient humans, making these cells auxotrophic for arginine, which opens a therapeutic perspective for the cure of hereditary leiomyomatosis and renal cell cancer |
729518 |
| 4.3.2.1 | medicine |
manipulating the enzyme expression or activity might be of potential benefit for treatment of necrotizing enterocolitis |
728938 |
