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 PDOC01037Methylglyoxal synthase active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC01037
Description
Methylglyoxal synthase (EC 4.2.3.3) (MGS) [1] catalyzes the conversion of dihydroxyacetone phosphate to methylglyoxal and phosphate. It provides bacteria with an alternative to triosephosphate isomerase for metabolizing dihydroxyacetone phosphate.
MGS is a small protein of about 13 to 17 kD. An aspartate residue is involved in the catalytic mechanism. We developed a signature pattern that includes that residue.
Last update:April 2006 / Pattern revised.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
Reference
| 1 | Authors | Saadat D. Harrison D.H.T. |
| Title | The crystal structure of methylglyoxal synthase from Escherichia coli. | |
| Source | Structure 7:309-317(1999). | |
| PubMed ID | 10368300 |
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