Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The plant cell cycle is equipped with two principal control points: PCP1 in G1 and PCP2 in G2 phase. These checkpoints can arrest the cell cycle in response to carbohydrate starvation, while sugar presence can revive the replication and mitotic activity. The process of cell cycle revival is strongly repressed by okadaic acid (OA) or 6-dimethylaminopurine (6-DMAP), inhibitors of specific protein phosphatases 1 or 2A or kinases (cyclin-dependent kinases), respectively. In the present study, it was investigated whether inhibition of cell cycle revival is performed through interference of the above-mentioned inhibitors with the metabolic pathway of sucrose applied to the cells. Changes of hexokinase (HK) and fructokinase (FK) activities, key enzymes of hexose metabolism, were analyzed in Vicia faba root meristem cells arrested in G1 and G2 phase by carbohydrate starvation as well as in those recovered with glucose or sucrose in the presence of OA or 6-DMAP. It was shown that in the sugar-starved cells, the activity of both enzymes decreased significantly. During cell regeneration with carbohydrates, the activity of HK was induced more by sucrose than by glucose, while FK remained inactive after glucose addition. Moreover, in situ investigation of the activities of HK and FK showed that OA-induced and 6-DMAP-induced repression of the cell cycle revival is connected with the interference of these drugs in the metabolic pathway of sucrose. It was also indicated that stronger OA-induced and 6-DMAP-induced inhibition of the replication and mitosis revival, at the early stages of sucrose regeneration, was correlated with the stronger influence of these inhibitors on HK and FK activities.
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PMID:In situ activities of hexokinase and fructokinase in relation to phosphorylation status of root meristem cells of Vicia faba during reactivation from sugar starvation. 1933 47

We have previously found that Drosophila melanogaster only has one deoxyribonucleoside kinase, Dm-dNK, however, capable to phosphorylate all four natural deoxyribonucleosides. Dm-dNK was originally isolated from an embryonic cell line. We wanted to study the expression of Dm-dNK during development from embryonic cells to adult flies and found declining Dm-dNK activity during development and no activity in adult flies. Surprisingly, the extract from adult flies exhibited a strong inhibitory effect on deoxyribonucloside kinase activity. The dNK-inhibitor was precipitable with ammonium sulfate, and was purified to a high degree by gel-filtration as indicated by LC-MS/MS analysis. Since the inhibitor eluted from G-200 gel-filtration with a size of 10-13 kDa, we named it P12. We tested the purified fraction for specificity towards various enzymes and found that both mammalian and bacterial dNKs were inhibited, whereas there was no effect on hexokinase and pyruvate kinases and acidic phosphatase. However, when tested against cyclin B-dependent kinase, we found a strong inhibitory effect. Both with human Cdk1/CycB and S. pombe Cdc2/B-type cyclin the purified fraction from Superdex 200 that inhibited Dm-dNK, also inhibited the two protein kinases to the same degree. Furthermore, testing P12 in a DNA polymerase based assay we found that the 3'-5'-exonuclease part of the DNA polymerase (Klenow polymerase) was activated.
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PMID:Isolation of a novel protein, P12-from adult Drosophila melanogaster that inhibits deoxyribonucleoside and protein kinase activities and activates 3'-5'- exonuclease activity. 2790 21