Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:1.5.1.3 (
dihydrofolate reductase
)
5,819
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The amount of
xanthine dehydrogenase
(
XDH
),
dihydrofolate reductase
(
DHFR
), and lactate dehydrogenase (LDH) in crude extracts of 4- to 5-day-old adult Aedes aegypti was determined, and the properties of these enzymes were partially characterized. It was then found that the amount and other selected characteristics of
XDH
and LDH in extracts of female Ae. aegypti processed 5 to 7 days and 12 to 14 days after they had fed upon either normal or Brugia pahangi-infected jirds were indistinguishable from those of these two enzymes in extracts of female mosquitoes that did not have a blood meal. Under the same circumstances, the selected characteristics of
DHFR
were also unaffected. However, there was a suggestion that the amount of
DHFR
was slightly increased in extracts of female Ae. aegypti processed 5 to 7 days after they had fed upon B. pahangi-infected jirds; by 12 to 14 days after the blood meal, there was a consistent 30% to 60% increase in the amount of
DHFR
inextracts of infected mosquitoes.
DHFR
activity could not be detected in a similarly prepared extract of 4,000 to 5,000 infective (L-3) B. pagangi larvae, the approximate number present in the infected mosquito extracts. It would appear, therefore, that the increased amount of turnover of
DHFR
in the mosquito host occurs in response to advanced infection with B. pahangi.
...
PMID:Comparative activity and properties of lactate dehydrogenase, xanthine dehydrogenase, and dihydrofolate reductase in normal and Brugia pagangi-infected Aedes aegypti. 55 68
Amide and ureide biogenic enzymes were measured in the plant fraction of soybean (Glycine max) nodules during the period 11 to 23 days after inoculation with Rhizobium japonicum (USDA 3I1b142). Enzymes involved in the initial assimilation of ammonia, i.e. glutamine synthetase, glutamate synthase, and aspartate aminotransferase, showed substantial increases in their specific activities over the time course. These increases paralleled the induction of nitrogenase activity in the bacteroid and leghemoglobin synthesis in the plant fraction. The specific activity of asparagine synthetase, however, showed a rapid decline after an initial increase in specific activity. Following the initial increases in the ammonia assimilatory enzymes, there was an increase in the activity of 5-phosphoribosylpyrophosphate amidotransferase, the enzyme which catalyzes the first committed step of de novo purine biosynthesis. This was followed by a dramatic increase in the purine oxidative enzymes,
xanthine dehydrogenase
and uricase. Smaller increases were observed in the activities of enzymes associated with the supply of metabolites to the purine biosynthetic pathway: phosphoglycerate dehydrogenase, serine hydroxymethylase, and methylene
tetrahydrofolate dehydrogenase
.The concentration of asparagine in the plant fraction decreased at the same time as the observed decrease in asparagine synthetase activity. This was followed by a recovery in plant fraction levels of asparagine in the presence of a continuing fall in the glutamine concentration and continued low asparagine synthetase activity.The data presented are consistent with initial assimilation of ammonia into glutamine and aspartate, which are metabolized by an elevation of endogenous purine biosynthetic enzymes, and then, by the induction of a specific group of purine oxidative enzymes, directed to allantoic acid production.
...
PMID:Enzymes of amide and ureide biogenesis in developing soybean nodules. 1666 97
Subcellular organelle fractionation of nitrogen-fixing nodules of soybean (Glycine max (L.) Merr.) indicates that a number of enzymes involved in the assimilation of ammonia into amino acids and purines are located in the proplastids. These include asparagine synthetase (EC 6.3.1.1), phosphoribosyl amidotransferase (EC 2.4.2.14), phosphoglycerate dehydrogenase (EC 1.1.1.95), serine hydroxymethylase (EC 2.1.2.1), and methylene-
tetrahydrofolate dehydrogenase
(EC 1.5.1.5). Of the two isoenzymes of asparate aminotransferase (EC 2.6.1.1) in the nodule, only one was located in the proplastid fraction. Both glutamate synthase (EC 1.4.1.14) and triosephosphate isomerase (EC 5.3.1.1) were associated at least in part with the proplastids. Glutamine synthetase (EC 6.3.1.2) and
xanthine dehydrogenase
(EC 1.2.1.37) were found in significant quantities only in the soluble fraction. Phosphoribosylpyrophosphate synthetase (EC 2.7.6.1) was found mostly in the soluble fraction, although small amounts of it were detected in other organelle fractions. These results together with recent organelle fractionation and electron microscopic studies form the basis for a model of the subcellular distribution of ammonium assimilation, amide synthesis and uredie biogenesis in the nodule.
...
PMID:Subcellular organization of ureide biogenesis from glycolytic intermediates and ammonium in nitrogen-fixing soybean nodules. 2427 25
