EC Number   |
General Information |
Reference |
|---|
    4.3.2.1 | malfunction |
a point mutation of a gene encoding argininosuccinate lyase causes a short root phenotype in the root elongation defect 1 mutant ref1, the enzyme activity is lost by the mutation R140L in OsASL1.1. The mutant has a shorter length from the quiescent center to the starting point of the elongation zone but a similar cell size and number of lateral and crown roots, and similar radial structure and nutrient uptake patterns compared to the wild-type. The mutant phenotype can be rescued by exogenous addition of arginine, but not by other amino acids |
730616 |
| 4.3.2.1 | malfunction |
an increase in aspartate- and citrulline-derived argininosuccinate is a consequence of enzyme inhibition by high levels of fumarate in fumarate hydratase-deficient cells. In these cells, argininosuccinate is not produced from citrulline and aspartate in FH-deficient cells but rather from arginine and fumarate |
729518 |
| 4.3.2.1 | malfunction |
argininosuccinate aciduria is observed in patients deficient in the enzyme. An increase in aspartate- and citrulline-derived argininosuccinate is a consequence of enzyme inhibition by high levels of fumarate in fumarate hydratase-deficient cells. In these cells, argininosuccinate is not produced from citrulline and aspartate in FH-deficient cells but rather from arginine and fumarate |
729518 |
| 4.3.2.1 | malfunction |
argininosuccinate lyase deficiency (ASLD) is a rare autosomal-recessive urea cycle defect caused by mutations in the ASL gene encoding argininosuccinate lyase. ASLD has a broad clinical spectrum ranging from life-threatening severe neonatal to asymptomatic forms. Different levels of residual ASL activity probably contribute to the phenotypic variability. All ASL mutations that are identified in patients with late onset or mild clinical and biochemical courses by ASL expression in human embryonic kidney are investigated |
748357 |
| 4.3.2.1 | malfunction |
argininosuccinic aciduria, ASA, MIM 207900, is the second most common human urea cycle disorder and is caused by deficiency of argininosuccinate lyase. Subjects with ASA disease cannot generate arginine from citrulline. Loss of the enzyme also leads to reduced NO synthesis due to decreased endogenous arginine synthesis as well as reduced utilization of extracellular arginine for NO production in humans |
730448 |
| 4.3.2.1 | malfunction |
loss of enterocyte-derived enzyme results in increased incidence of necrotizing enterocolitis, phenotype, overview |
728938 |
| 4.3.2.1 | malfunction |
loss of the enzyme leads to reduced NO synthesis due to decreased endogenous arginine synthesis as well as reduced utilization of extracellular arginine for NO production in mice. Enzyme hypomorphic mice show global NO deficiency and evidence of multi-organ dysfunction, phenotypes, hypomorphic mouse model of enzyme deficiency, overview |
730448 |
| 4.3.2.1 | metabolism |
as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis |
748357 |
| 4.3.2.1 | metabolism |
ASL synthesizes the second step in production of arginine, which is a part of the congenital urea cycle |
705506 |
| 4.3.2.1 | metabolism |
biological activity in liver, ileum, small intestine, heart, lung and kidney within the urea and nitric oxide cycle |
709968 |
