We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00153Delta-aminolevulinic acid dehydratase active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00153
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
PROSITE method (with tools and information) covered by this documentation:
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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