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 PDOC01029Diaminopimelate epimerase signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC01029
Description
Diaminopimelate epimerase (EC 5.1.1.7) catalyzes the isomeriazation of L,L- to D,L-meso-diaminopimelate in the biosynthetic pathway leading from aspartate to lysine.
This enzyme is a protein of about 30 Kd. Two conserved cysteines seem [1] to function as the acid and base in the catalytic mechanism. As a signature pattern, we selected the region surrounding the first of these two active site cysteines.
Last update:April 2006 / Pattern revised.
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Technical section
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Reference
| 1 | Authors | Cirilli M. Zheng R. Scapin G. Blanchard J.S. |
| Title | Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. | |
| Source | Biochemistry 37:16452-16458(1998). | |
| PubMed ID | 9843410 | |
| DOI | 10.1021/bi982138o |
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