Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ALDOLASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,063 records · Page 59Linked to original sources
PubMed1979

A new gene involved in expression of fructose-1,6-diphosphate aldolase activity in Escherichia coli.

A new gene, fdaB, has been mapped by transduction and partial diploid analyses and located adjacent to argA at 59.9 min on the Escherichia coli recalibrated linkage map. This gene is involved in expression of fructose-1,6-diphosphate aldolase activity and indirectly in ribosomal RNA synthesis. The temperature-sensitive mutant strain AA-157, containing the defective gene product of of fdaB, accumulates high concentrations of fructose 1,6-diphosphate at the nonpermissive temperature.

Chromosome Mapping↗
PubMed1976

The specific activity of aldolase in the livers of old and young rats.

The catalytic activity of liver fructose-biphosphate aldolase (EC 4.1.2.13) of young and old rats in units per manomole sequence has been calculated. No evidence of the accumulation with age of altered enzyme molecules of low catalytic activity was obtained. This is contrary to results obtained using mice and rabbits and indicates that the accumulation of altered enzymes may not always be associated with aging. The possibility that altered proteins are formed, but do not accumulate, cannot be ruled out.

Aging↗
PubMed2004

Isolation and transcriptional regulation of the Kluyveromyces lactis FBA1 (fructose-1,6-bisphosphate aldolase) gene.

Cloning and transcriptional regulation of the KlFBA1 gene that codes for the class II fructose-1,6-bisphosphate aldolase of the yeast Kluyveromyces lactis are described. KlFBA1 mRNA diminishes transiently during the shift from hypoxic to fully aerobic conditions and increases in the reversal shift. This regulation is mediated by heme since expression was higher in a mutant defective in heme biosynthesis. KlFBA1 transcription is not induced by calcium-shortage, low temperature, or at stationary phase. These data suggest that KlFBA1 plays a role in the balance between oxidative and fermentative metabolism and that this gene is differentially regulated in K. lactis and Saccharomyces cerevisiae, i.e., a respiratory vs. fermentative yeast.

Cloning, Molecular↗
PubMed1997

Microbial aldolases and transketolases: new biocatalytic approaches to simple and complex sugars.

Enzymes have become exceedingly valuable tools in organic synthesis as the reactions they catalyze generally proceed under mild conditions and in high stereo- and regioselectivity. Advances in microbiology and genetic engineering have greatly increased the availability of various enzymes. One of the most useful applications of enzyme-catalyzed chemical transformations is in the synthesis of water-soluble, polyfunctional organic molecules such as carbohydrates. As the pivotal roles that carbohydrates play in biological processes become more evident, access to these compounds becomes increasingly important. This review gives a brief overview of the use of aldolases and transketolases in the synthesis of sugars, sugar analogs, and related compounds.

Bacteria↗
PubMed2002

Conservation of avian Z chromosomes as revealed by comparative mapping of the Z-linked aldolase B gene.

A chicken Z-linked BAC probe containing the aldolase B gene was used for fluorescence in-situ hybridization (FISH) mapping in four different avian species. The biotinylated BAC clone showed distinct unique hybridization sites on the structurally different Z chromosomes. This result, together with previous data, lends credence to the notion that, despite undergoing structural rearrangements, the gene content of the avian Z chromosome remained conserved during evolution. Our study also demonstrates the feasibility of using large genomic clones for comparative mapping of Z-linked genes in birds.

Animals↗
PubMed2005

The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function.

The 911 amino acid band 3 (SLC4A1) is the major intrinsic membrane protein of red cells and is the principal Cl-/HCO3- exchanger. The N-terminal cytoplasmic domain of band 3 anchors the spectrin-based membrane skeleton to the lipid bilayer through its interaction with ankyrin and also binds glycolytic enzymes and hemoglobin. We identified a son of a consanguineous marriage with severe anemia in association with marked deficiency of band 3 (12% +/- 4% of normal). Direct nucleotide sequencing of SLC4A1 gene demonstrated a single base substitution (T --> C) at position + 2 in the donor splice site of intron 2, resulting in the generation of a novel mutant protein. Biochemical characterization of the mutant protein showed that it lacked the first 11 N-terminal amino acids (band 3 Neapolis). The expression of the mutant protein resulted in the complete absence of membrane-bound aldolase, and the mutant band 3 could not be tyrosine phosphorylated. The ability of the malarial parasite P falciparum to invade these red cells was significantly decreased. The identification of a novel band 3 mutant and its structural and functional characterization enabled us to identify pivotal roles for the 11 N-terminal amino acids in several protein functions and, in turn, in red-cell physiology.

Amino Acid Sequence↗
PubMed1997

Cell type- and positionally specific regulation of the aldolase P gene expression in rice seedlings.

We describe here different regulation of the AldP gene, a nuclear gene encoding chloroplast aldolase, in different tissues and growth ages of rice seedlings. Expression of the AldP gene is mesophyll cell-specific, and increases from the basal to the upper region in each leaf. The gene expression is repressed in the dark-grown leaf blade, but is induced by a short-term-exposure to light, to a level higher than that seen in the normal leaf blade. However, the light-inducibility differs among the tissues, and shows different patterns among leaf positions; i.e., the extent of light-induction is higher in the third leaf blade as compared with the earlier developed second leaf blade. Such positional differences in the regulation are also seen in the leaf sheath. These responses are not accompanied by changes of the cell type specificity in the expression.

Fructose-Bisphosphate Aldolase↗
PubMed2001

DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins.

Thermally aggregated, endogenous proteins in Escherichia coli cells form the S fraction, which is separable by sucrose density gradient centrifugation. To date, relatively little is known about the mechanisms of elimination of the heat-aggregated proteins from E. coli cells and the composition of the S fraction. We have identified several proteins of the S fraction using 2D-gel electrophoresis and microsequencing. A thermostable II class fructose-1,6-bisphosphate aldolase (Fda protein) appeared to be one of numerous proteins of the S fraction. Fda was purified from E. coli overproducer strain and used as a model substrate for investigation of the role of Hsps in prevention and repair of thermal denaturation of proteins both in vivo and in vitro. We found that the heat inactivation of Fda was reversible and that its reactivation in vivo and in vitro required mainly the assistance of the DnaK/DnaJ chaperone system. The dnaK756 and dnaJ259 mutations had a negative effect on the reactivation of thermally inactivated Fda. Moreover, we showed that the reactivation process in vitro was enhanced when GroEL/GroES were added together with DnaK/DnaJ. GroEL/GroES alone were inefficient in the resolubilization or reactivation of the heat-aggregated Fda. It is supposed that the denaturation of the thermostable Fda in vivo results rather from a temporary and transient deficit of Hsps than from the direct heat effect.

Cell Fractionation↗
PubMedDate not supplied

Cyanophora paradoxa: nucleotide sequence and phylogeny of the nucleus encoded muroplast fructose-1,6-bisphosphate aldolase.

Immunoscreening of a C. paradoxa expression library against water soluble muroplast ("cyanelle") proteins resulted in isolation of a clone encoding the nucleus-encoded muroplast class-II fructose-1,6-bisphosphate aldolase (class-II FBA). Its nucleotide sequence was determined. The 1432 bp insert, derived from a single-copy gene transcript, bears a reading frame of 1206 bp in length, representing 402 amino acids with 346 amino acids of mature protein. The leading amino acids match structural features necessary for precursor import across chloroplast envelope membranes. In phylogenetic tree topology, the investigated mature FBA clusters within type B FBAs with Synechocystis sp. as nearest neighbor. This is the first report of a Type B class-II FBA sequence of plastids.

Amino Acid Sequence↗
PubMed1983

[Studies on the serum aldolase activity in workers with muscle disorders caused by vibration work].

Recently, vibrating tools such as chain saws, pneumatic hammers, rock drills, riveters, and grinders have been widely introduced in various industries in order to increase efficiency and to reduce the burden of labor. The disease due to hand-arm vibration often causes serious damages to the operator's body, more particularly of the circulatory, peripheral nervous, osteo-articular and muscular systems. Many kinds of examinations such as roentgenography, electromyography, and sthenometry have been used to diagnose the damage to the musculoskeletal systems. Among these, the measurement of muscular strength, evaluated by grip and pinch strength, is widely used in mass examinations of vibration hazards but this is not always effective in precise recognition of the decrease in muscular strength. In the present study, therefore, in order to diagnose the severity of muscle disorders objectively, serum activities of aldolase (ALD), creatine phosphokinase (CPK) and lactate dehydrogenase (LDH), which are called "muscle enzymes," were determined in 260 chain saw operators aged 40 to 59 years. The same tests were performed for 46 healthy subjects (controls) of a similar age-range, who had a very short experience handling bush cleaners. All chain saw operators were classified into four groups according to the total chain saw operating time (TOT): 1) 58 operators with up to 2,500 hours' experience, 2) 70 with 2,500-5,000 hours' experience, 3) 74 with 5,000-10,000 hours' experience, and 4) 58 with over 10,000 hours' experience. The relationships were investigated in their enzyme activities on the one hand, and their TOT, muscular strength and numbness and pain symptoms related to muscle disorders of the upper extremities on the other hand. The following results were obtained: 1) Serum ALD and LDH activities in chain saw operators increased in proportion to the decrease in muscular strength. The activity of ALD showed a tendency to increase with increased TOT. The ALD activity in the group with over 5,000 hours' experience was significantly higher than that in the control group. However, no relationships were observed between CPK, LDH activities and TOT. 2) In chain saw operators with numbness and pain symptoms, ALD activity in the group with 2,500 hours' experience was significantly higher than that in the control group. However, no obvious relationships were found between CPK, LDH activities and numbness and pain symptoms. 3) In chain saw operators with muscular weakness in addition to numbness and pain symptoms, ALD activity in the group with over 2,500 hours' experience was significantly higher than that in the control group.(ABSTRACT TRUNCATED AT 400 WORDS)

Adult↗
PubMed2003

Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus.

In this study, we have crystallized class II fructose-1,6-bisphosphate aldolase (FBA) from Thermus caldophilus (Tca). Purified Tca FBA is a tetrameric enzyme of 305 residues, which crystallizes in the space group P2(1)2(1)2(1) (cell dimensions a = 98.9, b = 113.1, c = 115.7 A), with four molecules in the asymmetric unit. A complete diffraction data set was obtained from orthorhombic crystals at resolution of 2.2 A.

Amino Acid Sequence↗
PubMed2004

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.

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.

Acetyltransferases↗
PubMed1988

The quantification of eight enzymes from the ageing rat lens, with respect to sex differences and special reference to aldolase.

Eight enzymes, e.g. lactate dehydrogenase, malate dehydrogenase, fructose-diphosphate aldolase, sorbitol dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were estimated quantitatively in the rat lens from 37 to 1,211 days of age, by spectrophotometric methods. The activity was expressed as mU/g LWW. All enzymes measured showed declining activities, but LDH, ALD, SDH, G-6-PDH, HK and PFK gave a significant decrease during ageing when plotted semi-logarithmically from 37 to 1,211 days. SDH and G-6-PDH showed a statistically significant difference between the enzymes from the male and the female lenses. The female lens always had a lower activity than the male lens. Of all enzymes the specific activity, expressed as mU/l mg protein, was calculated. This specific activity appeared to be rather constant during ageing, except for ALD. In the female lenses, the specific activity of 7 enzymes was lower than in the male lenses. For ALD the specific activity decreased significantly in the male lens from 5.32 at 37 days to 0.88 at 1,211 days. In the female lens this significant decrease was from 4.97 to 0.81.

Aging↗
PubMed1975

Effect of fasting, phenobarbital, or hydrocortisone on serum creatine-phosphokinase and aldolase activity in myopathic Syrian hamsters.

The hereditary polymyopathy and cardiomyopathy of inbred Syrian hamsters (UM X 7.1) are associated with a marked elevation of serum creatine phosphokinase (CPK) and aldolase levels. Fasting (overnight) further increases (+100-500%) the serum concentration of these enzymes in myopathic hamsters; however, no such effect is demonstrable in normal hamsters, or in first generation offspring produced by crossbreeding the two strains (myopathic and normal). The changes are reversible, and the enzyme values return to previous levels within 72 hr. Neither phenobarbital nor hydrocortisone prevents the rises, as shown by CPK determinations; on the contrary, hydrocortisone elicits even greater serum enzyme increases.

Animals↗
PubMed1981

Influence of dietary fat on growth and liver lipid content, glucose-6-phosphate and 6-phosphogluconate dehydrogenases, and aldolase activities in the chick.

The influence of fat in chick diets containing 18, 21, and 24% protein on growth and liver lipid content, glucose 6-phosphate, and 6-phosphogluconate dehydrogenases, and aldolase activities was evaluated. Twelve percent fat in diets containing 21 and 24% protein increased the rate of growth. The fat level also decreased liver lipid content at 24% dietary protein. Improved growth was attributed to higher feed intake. However, dietary fat did not affect the activities of the above enzymes indicating their inadaptive nature to dietary fat.

Animals↗
PubMed1996

Using the process of reactive immunization to induce catalytic antibodies with complex mechanisms: aldolases.

The process of reactive immunization has been used to induce efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Reactive immunogens are those that react chemically during induction of the immune response. This same reaction is used later in catalysis. In essence one immunizes with the equivalent of a mechanism-based inhibitor. The difference is that instead of inhibiting a mechanism, a mechanism is induced. This advance allows the experimenter to dictate the exact mechanism by which catalytic antibodies proceed. The hapten used in the present study is a 1,3-diketone that both traps the requisite lysine residue to initiate formation of the enamine and induces a binding pocket that overcomes the entropic barrier of this bimolecular reaction.

Acetone↗
PubMedDate not supplied

[Changes in the primary structure of rabbit muscle aldolase under the influence of valine against a background of prolonged fasting].

The primary structure of the muscle aldolase molecule was studied as affected by semilethal doses of valine administered the abdominal cavity of the rabbits after a long fasting. It is established that in spite of differences in the amino acid composition of the protein, uniformity of the peptides distribution in the process of bromo-cyanogen fragments elution and the total amount of amino acid residues in the identical fragments are maintained. Changes are found only in the point-replacements by amino acids in C-fragment of the molecule (asparagine is replaced by valine and threonine by serine).

Amino Acid Sequence↗