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 PDOC00067Glucose-6-phosphate dehydrogenase active site
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00067
Description
Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) (G6PD) [1] catalyzes the first step in the pentose pathway, the reduction of glucose-6-phosphate to gluconolactone 6-phosphate. A lysine residue has been identified as a reactive nucleophile associated with the activity of the enzyme. The sequence around this lysine is totally conserved from bacterial to mammalian G6PD's and can be used as a signature pattern.
Last update:April 2006 / Pattern revised.
-------------------------------------------------------------------------------
Technical section
PROSITE method (with tools and information) covered by this documentation:
Reference
| 1 | Authors | Jeffery J. Persson B. Wood I. Bergman T. Jeffery R. Joernvall H. |
| Title | Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure. | |
| Source | Eur. J. Biochem. 212:41-49(1993). | |
| PubMed ID | 8444164 |
Copyright
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.