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)

In Arthrobacter pyridinolis, a respiration-coupled transport system for L-rhamnose caused accumulation of free L-rhamnose, while a phosphoenolpyruvate: L-rhamnose phosphotransferase system caused accumulation of L-rhamnose I-phosphate (Levinson & Krulwich, 1974). The pathways for subsequent metabolism of L-rhamnose and L-rhamose I-phosphate have now been investigated. Arthrobacter pyridinolis contains an inducible L-rhamnose isomerase and L-rhamnulokinase, as well as a constitutive L-rhamnulose I-phosphate aldolase. Results with mutants which are unable to metabolize L-rhamnose suggest the presence of an L-rhamnose I-phosphate phosphatase, which forms free L-rhamnose by hydrolysis of L-rhamnose I-phosphate produced by the phosphotransferase system. Mutants which lack this enzyme exhibited severe inhibition of growth in the presence of L-rhamnose plus any of a variety of carbon sources. There is some evidence that this inhibition was due to accumulation of L-rhamnose I-phosphate at toxic concentrations within the bacteria. The metabolism of L-rhamnose transported by the phosphotransferase system therefore appears to occur by hydrolysis of L-rhamnose I-phosphate to free L-rhamnose by a phosphatase. Metabolism of the L-rhamnose thus produced, and of that accumulated by the respiration-coupled transport system, the proceeds by the sequence of reactions: L-rhamnose leads to L-rhamnulose leads to L=rhamnulose I-phosphate leads to dihydroxyacetone phosphate plus L-lactaldehyde.
J Gen Microbiol 1976 Aug
PMID:Metabolism of L-rhamnose in Arthrobacter pyridinolis. 18 6

Changes in enzymes and metabolites of the carbohydrate metabolism in skeletal muscles were studied in mice after intracerebral inoculation of dengue type 2 virus. It was noted that lactic dehydrogenase, aldolase, phosphoglucoisomerase, phosphoglucomutase, GO-T and GP-T activity were enhanced initially by two- to three-fold, reaching a peak on day 5. As the illness appeared in mice, all the enzyme activities were lowered and were about three times less in the paralytic stage on the 8th day as compared to controls. Fructose-1,6-diphosphatase activity was increased on the 4th and 5th days but decreased later. Acid phosphatase increased abruptly from the 6th day while alkaline phosphatase activity was irregular. Creatine increased on the 4th and 5th days but diminished later. Glycogen decreased from the beginning and was lowest on the 5th day, but the levels increased later and were maximum in paralysed muscles. On the other hand, lactic acid began accumulating in the muscles and was maximum on the 5th day, then declined. Dengue virus was detected in the muscles from the 2nd day but higher titres were seen from the 6th day. Changes similar to the preparalytic stage of mice may occur in human beings, causing myalgia.
J Gen Virol 1978 Aug
PMID:Biochemical study of certain enzymes and metabolites of the carbohydrate metabolism in the skeletal muscle of the dengue virus-infected mice. 69 Jun 8

Polyacrylamide-disc gel electrophoresis and quantitative enzyme assays showed that the pathways of glucose catabolism and secondary metabolism in Penicillium expansum were dependent on the degree of aeration of the cultures. The isoenzyme patterns and specific activities of aldolase and succinate dehydrogenase indicated that glycolysis and the tricarboxylic acid cycle operated under conditions of both limited and efficient aeration (i.e. in cultures grown statically or on an orbital shaker). At high levels of aeration the growth rate was faster and synthesis of extracellular pectolytic enzymes was enhanced, whilst the activities of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase showed that the pentose-phosphate shunt was important in glucose catabolism during the trophophase of growth. In contrast, under conditions of low aeration this latter pathway was virtually undetectable, growth was slower, pectolytic enzyme production low and large concentrations of secondary metabolites (6-methylsalicylic acid, patulin and citrinin) accumulated.
J Gen Microbiol 1975 Aug
PMID:The effects of aeration on glucose catabolism in Penicillium expansum. 117 56

Thermotropic properties of liposome membranes prepared of bulk bovine erythrocyte membrane lipids, native, or aldolase-modified, were investigated by the ESR method. Breaks were observed in the log 2T parallel vs 1/T plots for two spin labels: tempopalmitate and 5-doxyl-palmitate methyl ester. These phenomena have been interpreted as reflecting structural changes near the lipid bilayer polar heads region. Upon modification with aldolase, the temperature at which the breaks occurred was decreased for both spin probes.
Gen Physiol Biophys 1989 Dec
PMID:The interaction of fructose-1,6-biphosphate aldolase with liposome membranes: a spin probe technique study. 255 46

Anaerobiosis results in the selective synthesis of a particular set of polypeptides in the maize root including the two alcohol dehydrogenases (Sachs, M. M., Freeling, M., and Okimoto, R. (1980) Cell 20, 761-768), pyruvate decarboxylase (Wignarajah, K., and Greenway, H. (1976) New Phytol. 77, 575-584; Laszlo, A., and St. Lawrence, P. (1983) Mol. Gen. Genet. 192, 110-117), glucose phosphate isomerase (Kelley, P. M., and Freeling, M. (1984) J. Biol. Chem. 259, 673-677) and aldolase (Kelley, P. M., and Freeling, M. (1984) J. Biol. Chem. 259, 14180-14183). This report describes the identification and characterization of cDNA clones to five different mRNA species induced upon anaerobic shock. Immunoprecipitation of hybrid-selected translation polypeptides has determined the identity of the cDNA clone for fructose-1,6-diphosphate aldolase mRNA. Quantitative hybridization analysis of anaerobic mRNAs using the cDNA clones has shown that there is not a simultaneous accumulation of anaerobic mRNAs. Upon reintroduction of air, the anaerobic mRNAs disappear rapidly and at approximately the same rate. A translocation line that generates progeny that contain 1, 2, and 3 doses of the long arm of chromosome one (1L) allowed us to test for clustering of the anaerobic genes; two of the anaerobic genes tested do not reside with Adh 1 and Phi 1 on the long arm of chromosome 1.
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PMID:Coordinate induction of alcohol dehydrogenase 1, aldolase, and other anaerobic RNAs in maize. 258 Aug 29

Mutants of mucoid Pseudomonas aeruginosa defective in fructose-bisphosphate aldolase (FBA), NADP-linked glyceraldehyde-3-phosphate dehydrogenase (GAP) or 3-phosphoglycerate kinase (PGK) were unable to grow on gluconeogenic precursors like glutamate, succinate or lactate. The gap and pgk mutants could grow on glucose, gluconate or glycerol, but fba mutants could not. This suggests that the metabolism of glucose or gluconate does not require either PGK or NADP-linked GAP but does require the operation of the aldolase-catalysed step. For gluconeogenesis, however, all three steps are essential. Recombinant plasmids carrying genes for FBA, PGK, GAP or phospho-2-keto-3-deoxygluconate aldolase (EDA) activities were constructed from a genomic library of mucoid P. aeruginosa selecting for complementation of deficiency mutations. Analysis of their complementation profile indicated that one group of plasmids carried fba and pgk genes, while another group carried eda, 6-phosphogluconate dehydratase (edd) and glucose-6-phosphate dehydrogenase (zwf) genes. The gap gene was not linked to any of these markers. Partial restoration of FBA activity in spontaneous revertants of Fba- mutants was accompanied by a concomitant loss of PGK activity. These experiments indicate a linkage between the fba and pgk genes on the P. aeruginosa chromosome.
J Gen Microbiol 1987 Apr
PMID:Gluconeogenic mutations in Pseudomonas aeruginosa: genetic linkage between fructose-bisphosphate aldolase and phosphoglycerate kinase. 311 66

The requirement for gluconeogenesis and the pentose phosphate pathway in sporulation of Saccharomyces cerevisiae was investigated using homozygous diploids with mutations in selected portions of the respective metabolic pathways. Mutations affecting the genes FBA1 (fructose-1,6-bisphosphate aldolase), GPM1 (phosphoglycerate mutase) and ZWF1 (glucose-6-phosphate dehydrogenase) were used. Homozygous diploids bearing either fba1-11 or gpm1 mutations were asporogenous, indicating an absolute requirement for gluconeogenesis in sporulation. A strain homozygous for the zwf1 mutation sporulated, but at a reduced level compared to the wild-type. Homozygous spd1-1 mutations restored the ability to sporulate in fba1-11 homozygous diploids; this is believed to occur as a consequence of reduced NH+4 levels in spd1-1-bearing strains, the reduced intracellular NH+4 content serving to promote gluconeogenesis via the residual low levels of enzyme activity present in such mutants.
J Gen Microbiol 1986 Sep
PMID:A genetic and biochemical analysis of the role of gluconeogenesis in sporulation of Saccharomyces cerevisiae. 354 Feb 6

A panel of clones of mink-Chinese hamster somatic cell hybrids was analysed to obtain data for assigning the genes for thymidine kinase-1 (TK1), galactokinase (GALK), subunit C of aldolase (ALDC), and esterase D (ESD) to specific mink chromosomes. The results demonstrate that the genes for TK1, GALK, ALDC and ESD are syntenic and located on mink chromosome 8. Prometaphase analysis of transformed mouse cells obtained by transfer of mink genes by means of metaphase chromosomes demonstrated the presence of mink chromosome 8 fragments of different sizes in some of the independent transformants. Segregation analysis of these fragments and mink TK1, GALK, ALDC and ESD allowed us to assign the genes for TK1 and GALK to 8p24, ALDC to pter-8p25, and ESD to 8q24-8qter.
Mol Gen Genet 1985
PMID:Regional assignment of the genes for TK1, GALK, ALDC, and ESD on chromosome 8 in the American mink by chromosome-mediated gene transfer. 386 31

Phospho-2-keto-3-deoxy-heptonate aldolase (DAHP synthase) of Pseudomonas aureofaciens ATCC 15926 was inhibited by L-tyrosine. The inhibition was competitive with erythrose 4-phosphate as the varied substrate but non-competitive with respect to phosphoenolpyruvate. Anthranilate synthase was inhibited by L-tryptophan. The inhibition was competitive with respect to chorismate but non-competitive with L-glutamine or NH4+ as the varied substrate. DAHP synthase and anthranilate synthase were not repressed when aromatic amino acids were included in the growth medium. In bacteria grown in the presence of L-phenylalanine, the anthranilate synthase activity was enhanced about threefold compared with the control. Similar results were obtained with the mutant strain P. aureofaciens ACN, which produces increased amounts of pyrrolnitrin.
J Gen Microbiol 1980 Dec
PMID:Regulation of phospho-2-keto-3-deoxy-heptonate aldolase (DAHP synthase) and anthranilate synthase of Pseudomonas aureofaciens. 611 83

Anaerobically grown Staphylococcus epidermidis fermented glucose with the production of lactate and trace amounts of acetate, formate and CO2. Isotopic and inhibitor studies, assays for key enzymes of different metabolic pathways, and fermentation balances, all indicated that glucose was metabolized principally via glycolysis and to a very limited extent by the hexose monophosphate oxidative pathway. Serine fermentation proceeded via deamination and dismutation yielding NH3 and equimolar amounts of lactate, acetate and CO2; small amounts of formate arose by the operation of pyruvate-formate lyase. Incorporation of 0.5% (w/v) glucose in the growth medium depressed serine metabolism by repressing the activities of serine dehydratase and pyruvate dehydrogenase but, conversely, enhanced the activities of phosphofructokinase and lactate dehydrogenase. Glucose-grown organisms at various stages of anaerobic batch growth showed an inverse relationship between the rates of fermentation of serine and glucose. L-Lactate dehydrogenase activity in crude extracts depended on fructose 1,6-bisphosphate, and fructose 1,6-bisphosphate aldolase was found to be a class I aldolase. Despite the presence of ribokinase, D-ribose-5-phosphate isomerase, transaldolase and transketolase, the organisms utilized ribose only after growth aerobically in basal medium, and then at a slow rate after an initial lag period.
J Gen Microbiol 1980 May
PMID:Anaerobic glucose and serine metabolism in Staphylococcus epidermidis. 677 45


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