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 PDOC01000Dihydrodipicolinate reductase signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC01000
Description
Dihydrodipicolinate reductase (EC 1.3.1.26) catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate. This enzyme is present in bacteria (gene dapB) and higher plants.
As a signature pattern we selected the best conserved region in this enzyme. It is located in the central section and is part of the substrate-binding region [1].
Last update:December 2004 / Pattern and text revised.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
Reference
| 1 | Authors | Scapin G. Blanchard J.S. Sacchettini J.C. |
| Title | Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. | |
| Source | Biochemistry 34:3502-3512(1995). | |
| PubMed ID | 7893645 |
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