Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

The rice genome contains at least four separate loci that encode aldolase isozymes. Among these, the aldolase P (AldP) gene, a nuclear gene coding for chloroplast aldolase, is expressed predominantly in the leaf blade mesophyll cells in rice. To dissect promoter elements that regulate such tissue- or cell type-specific expression, we constructed various AldP promoter-beta-glucuronidase (GUS) fusion genes and transferred them into Nicotiana tabacum (tobacco) plants. Analysis of GUS activities in the transgenic tobacco revealed the presence of at least two elements within 2.0 kb AldP promoter region. One is located within the segment from position -2.0 kb to -1.2 kb and acts as a negative element. The other is a positive element located between -1.2 kb and -0.31 kb that confers developmentally regulated, mesophyll cell-specific expression. In addition, the 1.2 kb rice promoter segment flanking the transcription start site contains an element(s) that serves as target for light induction in tobacco. The results suggest that the AldP gene promoter of rice, a monocot promoter, can function in an essentially physiological manner in the dicot tobacco plant.
Mol Gen Genet 1995 Oct 25
PMID:The promoter from the rice nuclear gene encoding chloroplast aldolase confers mesophyll-specific and light-regulated expression in transgenic tobacco. 747 69

Genomic clones encoding the plastidic fructose-1,6-bisphosphate aldolase of Chlamydomonas reinhardtii were isolated and sequenced. The gene contains three introns which are located within the coding sequence for the mature protein. No introns are located within or near the sequence encoding the transit-peptide, in contrast to the genes for plastidic aldolases of higher plants. Neither the number nor the positions of the three introns of the C. reinhardtii aldolase gene are conserved in the plastidic or cytosolic aldolase genes of higher plants and animals. The 5' border sequences of introns in the aldolase gene of C. reinhardtii exhibit the conserved plant consensus sequence. The 3' acceptor splice sites for introns 1 and 3 show much less similarity to the eukaryotic consensus sequences than do those of intron 2. The plastidic aldolase gene has two tandemly repeated CAAT box motifs in the promoter region. Genomic Southern blots indicate that the gene is encoded by a single locus in the C. reinhardtii genome.
Mol Gen Genet 1995 Aug 30
PMID:The plastid aldolase gene from Chlamydomonas reinhardtii: intron/exon organization, evolution, and promoter structure. 756 12

We used the minitransposon TnhlyAs [Gentschev, I., Maier, G., Kranig, A. and Goebel, W. (1996) Mol. Gen. Genet. 252, 266-274] for random insertion of the secretion signal (HlyAs) of Escherichia coli hemolysin (HlyA) into chromosomal genes. Four mini-TnhlyAs derivatives bearing the gltA (citrate synthase), deoC (2 deoxyribose-5 phosphate aldolase), tig (trigger factor) genes and an unknown ORF fused to hlyAs were identified and characterized. Our data suggest that TnhlyAs-generated hemolysin fusion proteins are secreted efficiently by the HlyB/HlyD/TolC hemolysin secretion machinery and that this can be useful for studies of gene expression or function.
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PMID:Construction of chromosomally encoded secreted hemolysin fusion proteins by use of mini-TnhlyAs transposon. 971 56

The effect of sodium acetate was studied on the change of the growth yield, the production of L- and D-lactic acid, and the activity of lactate dehydrogenases (LDHs; L-lactate dehydrogenase [EC 1.1.1.27, L-LDH] plus D-lactate dehydrogenase [EC 1.1.1.28, D-LDH]), fructose-1, 6-bisphosphate aldolase [EC 4.1.2.13, FBP-aldolase], and phosphofructokinase [EC 2.7.1.11, PFK] of Lactobacillus sakei NRIC 1071(T) and Lactobacillus plantarum NRIC 1067(T). The growth yield of L. sakei NRIC 1071(T) was increased 1.6 times in the presence of sodium acetate compared with its absence. The activity of LDHs in L. sakei NRIC 1071(T) and L. plantarum NRIC 1067(T) was retained longer under the addition of sodium acetate in the reaction mixture. As a result, these strains produced much more lactic acid in the presence of sodium acetate compared with its absence. Furthermore, the activity of L-LDH in L. sakei NRIC 1071(T) cultivated in the presence of sodium acetate increased three times or more compared with the activity of the cells cultivated in its absence. Consequently, the type of stereoisomers of lactic acid produced by L. sakei shifted from the DL-type to the L-type because the ratio of L-lactic acid to D-lactic acid produced became larger with the addition of sodium acetate to culture media. This phenomenon was not observed in L. plantarum NRIC 1067(T). Further, the participation of lactate racemase is discussed from the viewpoint of the production of D-lactic acid by L. sakei.
J Gen Appl Microbiol 2002 Apr
PMID:The effect of sodium acetate on the growth yield, the production of L- and D-lactic acid, and the activity of some enzymes of the glycolytic pathway of Lactobacillus sakei NRIC 1071(T) and Lactobacillus plantarum NRIC 1067(T). 1246 5

Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) was purified 97-fold from a halophilic archaebacterium Haloferax mediterranei, with a specific activity of 2.8. The enzyme was characterized as a Class II aldolase on the basis of its inhibition by EDTA and other metal chelators. The enzyme had a specific requirement for divalent metal Fe(2+) for activity. Sulfhydryl compounds enhanced aldolase activity.
J Gen Appl Microbiol 1998 Aug
PMID:A Class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei. 1250 17

1. A procedure for isolating nuclei of the wheat germ in non-aqueous media has been described. 2. Such nuclei were shown to constitute about 50 per cent of the protoplasmic mass and to have a ribonucleic acid content of an order equivalent to that of the cytoplasm. 3. Studies of the distribution of the enzymes-aldolase, phosphoglyceraldehyde dehydrogenase, enolase, and pyruvate kinase-have revealed that the nuclei are the most vigorous sites of glycolytic activity. 4. Analysis of the DPN content of the nuclei in calf tissues-liver, pancreas, and heart-pointed to the probability that glycolytic activity is a characteristic common to many nuclei. 5. The significance of glycolytic activity to nuclear function has been discussed and some suggestive comparisons made between the two energy-yielding systems of glycolytic and oxidative phosphorylation.
J Gen Physiol 1952 Nov
PMID:The isolation of wheat germ nuclei and some aspects of their glycolytic metabolism. 1301 Dec 76

It has been shown that helium has the ability to affect variously the rates of certain metabolic reactions in vitro as compared to nitrogen. An attempt has been made to approximate the sites of action in mouse liver preparations. The following results have been obtained by the substitution of a mixture of 80 per cent helium and 20 per cent oxygen for air: (a) An increase in the rate of oxygen consumption and carbon dioxide production to the same degree, the respiratory quotient remaining unchanged. (b) A decrease in the magnitude of cyanide inhibition. The effectiveness of helium increases with the degree of the cyanide inhibition. (c) No effect on the activity of slices which have been poisoned with fluoride when either lactate or pyruvate has been added as a substrate. (d) A change in the rate, and the slope of the curve of oxygen consumption in liver homogenates which are utilizing pyruvate as a substrate. The use of helium relative to nitrogen under anaerobic conditions causes: (a) A depression of the glycolytic rates in both mouse liver slices and diaphragm. (b) An increase in the carbon dioxide evolution and lactic acid production of mouse liver homogenates oxidizing either glucose and hexose diphosphate, or hexose diphosphate alone. In neither slices nor homogenates does the addition of fluoride and the use of pyruvate as the hydrogen acceptor alter the fundamental response of the preparations. The following hypotheses have been advanced and discussed in order to explain the observed phenomena: 1. Helium does not alter the substrate utilized by the tissue. 2. The gas interferes in some way with the cyanide-cytochrome oxidase bond, but may not affect cytochrome oxidase in the absence of cyanide. 3. The citric acid cycle is not subject to the influence of helium in tissue slices, but is altered in an unexplained fashion in homogenates. It is postulated that a rearrangement of particulate surfaces may be the significant factor here. 4. The glycolytic cycle is the site of both an inhibitory and an acceleratory effect of helium. The locus of the inhibition lies above the aldolase reaction and that of the acceleration between the aldolase and enolase reactions.
J Gen Physiol 1953 Mar
PMID:Effect of helium on the respiration and glycolysis of mouse liver slices. 1303 67

1. The C(14)O(2) production by Arbacia eggs and embryos from glucose-1-C(14), glucose-2-C(14), and glucose-6-C(14) has been measured without and with dinitrocresol in the incubation medium. In the absence of the dinitrocresol, the C(14)O(2) production from glucose-1-C(14) is more rapid than from glucose-2-C(14) and much more rapid than from glucose-6-C(14); this, together with previous findings, indicates that glucose is utilized in Arbacia eggs predominantly via the TPN shunt rather than via the aldolase step of the glycolytic pathway. In the presence of the dinitrocresol, C(14)O(2) from glucose-6-C(14) approaches that from glucose-1-C(14), indicating that, in the presence of this reagent, glucose utilization is diverted from the shunt to the glycolytic pathway. 2. Incorporation of C(14) from glucose labelled in the 1-, 2-, or 6- positions into other metabolic products of the eggs and embryos is also inhibited by dinitrocresol, particularly incorporation into the acid-insoluble fraction containing nucleoproteins.
J Gen Physiol 1956 Sep 20
PMID:Alteration by dinitrocresol of pathways for glucose oxidation in eggs of arbacia punctulata. 1335 35

Methods for measurement of glyceraldehyde-P dehydrogenase, triose-P isomerase, fructose 1,6-diphosphate aldolase, and the DPN-linked and flavin-linked alpha-glycero-P dehydrogenases in small amounts of tissue have been worked out. These enzymes have been measured in ten tracts in rabbit central nervous system. The activities of all the enzymes measured, except the flavin-linked alpha-glycero-P dehydrogenase, are present in larger amounts in lightly myelinated than in heavily myelinated tracts, but are relatively low in fibrillar layer of olfactory bulb, which is unmyelinated. Aldolase, like P-fructokinase (measured previously), is especially low in fibrillar layer. Taken together with relatively high 6-P-gluconate dehydrogenase activity found earlier this supports the hypothesis that the pentose-P shunt is particularly active in this tract. The activity of DPN-linked alpha-glycero-P dehydrogenase is inversely proportional to the lipid content of the myelinated tracts, which suggests that its primary role is not related to lipid synthesis in adult brain. The activities of flavin-linked alpha-glycero-P dehydrogenase are unrelated to those of the DPN-linked enzyme, which is contrary to expectation if the two enzymes function as partners in the "alpha-glycerophosphate shuttle."
J Gen Physiol 1964 Jan
PMID:QUANTITATIVE STUDIES OF WHITE MATTER. II. ENZYMES INVOLVED IN TRIOSE PHOSPHATE METABOLISM. 1410 Sep 62

Whether fructose-1,6-bisphosphate (FBP) triggers the transcriptional regulation of the gene expression of lactate dehydrogenase (LDH) and pyruvate formate-lyase (PFL) in Streptococcus bovis was examined by constructing a recombinant strain that overexpresses FBP aldolase (FBA). When the recombinant strain was grown on glucose, intracellular FBP was much lower as compared to the parent strain, whereas dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (GAP) were slightly higher. Intracellular ATP and ADP were slightly lower, but the NADH/NAD(+) ratio was not different. When glucose was replaced by lactose, a less readily utilized substrate, there was no great difference in FBP, DHAP, GAP, or adenine nucleotides. Overexpression of FBA decreased the level of LDH-mRNA, and increased the level of PFL-mRNA. Consequently, FBP concentration was positively related to the LDH-mRNA level and inversely related to the PFL-mRNA level. On the contrary, DHAP and GAP concentrations were positively related to the PFL-mRNA level and inversely related to the LDH-mRNA level. The levels of these mRNA were proportional to the amounts of corresponding enzymes in cells. As a result, the ratio of formate to lactate produced was increased by the overexpression of FBA. From these results, it could be presumed that FBP is involved in the transcriptional control of LDH and PFL synthesis in S. bovis.
J Gen Appl Microbiol 2004 Apr
PMID:Effects of the overexpression of fructose-1,6-bisphosphate aldolase on fermentation pattern and transcription of the genes encoding lactate dehydrogenase and pyruvate formate-lyase in a ruminal bacterium, Streptococcus bovis. 1524 45


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