EC Number   |
General Information |
Reference |
|---|
    2.7.1.40 | evolution |
14 putative pyruvate kinase genes are encoded by the Arabidopsis thaliana genome. Determination of five cytosol-localized pyruvate kinases, out of the fourteen putative pyruvate kinase genes encoded by the Arabidopsis thaliana genome, phylogenetic analysis. The five identified cytosolic pyruvate kinase isoforms adjust the carbohydrate flux through the glycolytic pathway in Arabidopsis thaliana, by distinct regulatory qualities, such as individual expression pattern as well as dissimilar responsiveness to allosteric effectors and enzyme subgroup association |
762193 |
| 2.7.1.40 | evolution |
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum |
-, 760784 |
| 2.7.1.40 | evolution |
enzyme EhPyk is the shortest Pyk known to date as it contains only two of the three characterized domains when compared to the other homologues, phylogenetic analysis, the enzyme belongs to a distinct branch from the known type I/II Pyks |
760635 |
| 2.7.1.40 | evolution |
significant evolutionary distance existing between the type I and type II isoenzymes in Gram-negative bacteria |
-, 721624 |
| 2.7.1.40 | malfunction |
aberrant growth factor signalling and oxidative stress inhibit PKM2, which results in the diversion of glucose carbons into anabolic and redox regulating pathways that are essential for cell growth and survival. Proliferating PKM2-null tumour cells have no detectable PK expression, which likely reflects an adaptation that suppresses expression of PKM1 in these tumours. Consistent with a negative role of high PK activity in tumour growth, both exogenous expression of PKM1 or pharmacological activators that overcome endogenous PKM2-inhibiting mechanisms impede tumour growth by increasing cellular PK activity, effectively rendering endogenous PKM2 into a PKM1-like enzyme |
761063 |
| 2.7.1.40 | malfunction |
allosteric site structure analysis of wild-type and mutant enzymes, overview. In the S531E variant glutamate binds in place of the 6'-phosphate of fructose-1,6-bisphosphate in the allosteric site, leading to partial allosteric activation. The structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant |
760301 |
| 2.7.1.40 | malfunction |
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation |
-, 760784 |
| 2.7.1.40 | malfunction |
consequence of PKM2 inhibition is a reduced glycolytic flux, which can be reflected by the rates of cellular glucose consumption and lactate production |
721966 |
| 2.7.1.40 | malfunction |
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases |
-, 760784 |
| 2.7.1.40 | malfunction |
depletion of isoform PKM2 suppresses the proliferation of Hep-G2 and Huh-7 cells and enhances the activities of the epidermal growth factor/epidermal growth factor receptor and transforming growth factorbetA1/transforming growth factor receptor signaling pathways |
739755 |
