EC Number   |
Natural Substrates |
|---|
    4.2.1.24 | 2 5-aminolevulinate |
- |
| 4.2.1.24 | 5-aminolevulinate |
- |
| 4.2.1.24 | 5-aminolevulinate |
during erythropoiesis in chordates the enzyme functions as a part of the heme synthesizing machinery |
| 4.2.1.24 | 5-aminolevulinate |
second enzyme in the heme biosynthetic pathway |
| 4.2.1.24 | 5-aminolevulinate |
the second and rate-limiting enzyme of the heme-biosynthetic pathway |
| 4.2.1.24 | 5-aminolevulinate |
induction by 17beta-estradiol of 5-aminolevulinate |
| 4.2.1.24 | 5-aminolevulinate |
enzyme catalyzes the first common step in tetrapyrrole biosynthesis |
| 4.2.1.24 | 5-aminolevulinate + 5-aminolevulinate |
essential step in tetrapyrrole biosynthesis |
| 4.2.1.24 | 5-aminolevulinate + 5-aminolevulinate |
the enzyme catalyzes the first common step in the biosynthesis of tetrapyrroles |
| 4.2.1.24 | 5-aminolevulinate + 5-aminolevulinate |
the enzyme catalyzes the third step of tetrapyrrole synthesis leading to the formation of heme and chlorophylls in plant tissues. In the light, both 5-aminolevulinate dehydratase activity, and protein level increases 3-4 times compared to the dark-control level. However, no change in the amount of related mRNA is observed. The apparent stability of the mRNA can be due to the abundant expression of a housekeeping gene, which shadows a related gene expressed in the light |
