PROSITE documentation PDOC00153Delta-aminolevulinic acid dehydratase active site
Description
Delta-aminolevulinic acid dehydratase (EC 4.2.1.24) (ALAD) [1] catalyzes the second step in the biosynthesis of heme, the condensation of two molecules of 5-aminolevulinate to form porphobilinogen. The enzyme is an oligomer composed of eight identical subunits. Each of the subunits binds an atom of zinc or of magnesium (in plants). A lysine has been implicated in the catalytic mechanism [2]. The sequence of the region in the vicinity of the active site residue is conserved in ALAD from various prokaryotic and eukaryotic species.
Last update:November 1995 / Pattern and text revised.
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Technical section
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References
| 1 | Authors | Li J.-M. Russell C.S. Cosloy S.D. |
| Title | The structure of the Escherichia coli hemB gene. | |
| Source | Gene 75:177-184(1989). | |
| PubMed ID | 2656410 |
| 2 | Authors | Gibbs P.N.B. Jordan P.M. |
| Title | Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. | |
| Source | Biochem. J. 236:447-451(1986). | |
| PubMed ID | 3092810 |
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