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 PDOC60002Phosphoketolase signatures
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC60002
Phosphoketolases are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Pks catalyze an irreversible thiamine diphosphate (ThDP) dependent phosphorolytic reaction splitting D-xylulose 5-phosphate (EC 4.1.2.9) or D-fructose 6-phosphate (EC 4.1.2.22) in the presence of inorganic phosphate to yield acetyl phosphate and glycerol 3-phosphate or erythrose 4-phosphate, respectively [1].
A multiple alignment of PK sequences shows several highly conserved regions. We selected two of these regions as signature patterns for PKs. The function of the first one is not known, whereas the second correspond to the ThDP binding site [1].
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Rohr L.M. Teuber M. Meile L. |
| Source | Chimia 56:270-273(2002). |
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.