Gene/Protein
Disease
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Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
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Query: EC:4.1.2.13 (
aldolase
)
3,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Clostridium thermocellum was shown to ferment glucose in a medium containing salts and 0.5% yeast extract. An active glucokinase was obtained with improved conditions for growth, assay, and preparation of cell extracts. Cell extracts appear to contain a glucokinase inhibitor that interferes with the assays at high protein concentrations.
Glucokinase
activity is stimulated about 60% by pretreatment with dithiothreitol. Little or no fructokinase or mannokinase activity was detected in cell extracts. The absence of glucokinase in mannitol-grown cells, the increase in glucokinase activity upon incubation of cell suspensions with glucose, and the lack of increase in activity when chloramphenical is added are evidence that glucokinase is an inducible enzyme. The following enzymes were detected in cell extracts (the enzyme activities are shown in parentheses are micromoles per minute per milligram or protein at 27 C): glucokinase (0.48), phosphoglucose isomerase (0.73), fructose 6-phosphate kinase (0.24),
fructose diphosphate aldolase
(0.59), glyceraldehyde 3-phosphate dehydrogenase (0.53), triose phosphate isomerase (0.13), phosphoglycerate kinase (0.20), phosphoglycerate mutase (0.20), enolase (0.28), pyruvic kinase (0.13), and lactic dehydrogenase (0.13). Glucose 6-phosphate dehydrogenase activity was absent or very low (0.0002) and 6-phosphogluconate dehydrogenase activity also was relatively low (0.015). From these data, it is proposed that carbohydrate metabolism in C. thermocellum proceeds by the Embden-Meyerhof pathway.
...
PMID:Utilization of glucose by Clostridium thermocellum: presence of glucokinase and other glycolytic enzymes in cell extracts. 554 Oct 8
Sugar metabolism in kernels of starch-deficient endosperm mutants of maize (Zea mays L.) was examined to determine how single locus mutations of carbohydrate metabolism affect carbohydrate metabolism as a whole. Activities of 14 enyzmes were measured in extracts from endosperms from isogenic lines of normal, shrunken, shrunken-2, shrunken-4, brittle-1, and brittle-2 maize in an OH43 background. Nearly every enzyme activity examined was affected in some or all of the mutants. Sucrose synthase and
aldolase
activities were lower in all mutants compared to normal. ADP-Glc pyrophosphorylase activity in immature kernels was much higher in brittle endosperms than in normal, but absent in brittle-2 and shrunken-2 endosperms. The activity in those genotypes exhibiting activity was positively correlated with sucrose concentration in the kernels. Sucrose may be modulating the coarse control of ADP-Glc pyrophosphorylase activity by affecting the genetic transcription of message for this enzyme. Sorbitol dehydrogenase activity was negatively correlated with its substrate, fructose, supporting the hypothesis that sorbitol dehydrogenase converts fructose produced during sucrose degradation into sorbitol.
Glucokinase
activity was positively correlated with mature kernel dry weight. This supports the hypothesis that glucokinase activity may limit sucrose utilization. Shrunken-4 extracts had lower activities for a number of enzymes, supporting the view that this mutant may have an impediment to protein synthesis. Elevated sucrose levels were evenly distributed throughout 20-day postpollination shrunken-2 kernels, whereas a sucrose concentration gradient existed in normal kernels between the basal region and the upper endosperm. This gradient is apparently generated by the utilization of sugars and may facilitate the movement of sugars into developing corn kernels.
...
PMID:Sugar metabolism in developing kernels of starch-deficient endosperm mutants of maize. 1666 16