| 别名 |
5-aminolaevulinic acid dehydratase, 5-aminolevulinate dehydrase, 5-aminolevulinate dehydratase, 5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), 5-aminolevulinic acid dehydrase, 5-aminolevulinic acid dehydratase, 5-levulinic acid dehydratase, Al-D, ALA dehydratase, ALA synthetase, ALA-D, ALAD, ALADH, aminolevulinate dehydrase, aminolevulinate dehydratase, aminolevulinic dehydratase, CF-2, d-ALAD, delta aminolevulinic acid dehydratase, delta-ALA-D, delta-ALAD, delta-aminolevulinate dehydrase, delta-aminolevulinate dehydratase, delta-aminolevulinate dehydrataseALAD, delta-aminolevulinic acid dehydrase, delta-aminolevulinic acid dehydratase, delta-aminolevulinic dehydratase, gamma-aminolevulinic acid dehydratase, HemB, PaPBGS, PBG synthase, PBG-S, PBG-synthase, PBGS, Pcal_1709, PfALAD, PGBS, Porphobilinogen synthase, porphobilinogen synthetase, synthase, porphobilinogen, TgPBGS |
| Comments |
The enzyme catalyses the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. The enzymes from most organisms utilize metal ions (Zn2+, Mg2+, K+, and Na+) as cofactors that reside at multiple sites, including the active site and allosteric sites. Enzymes from archaea, yeast, and metazoa (including human) contain Zn2+?at the active site. In humans, the enzyme is a primary target for the environmental toxin Pb. The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation. |
