Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
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Query: EC:2.7.1.1 (
hexokinase
)
5,274
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
An enzyme analysis of diploid and triploid Paragonimus westermani was conducted using starch gel electrophoresis. In total, 16 enzymes, probably encoded by 18 loci, were studied for 3 populations of the diploid form sampled from 2 localities, and 4 populations of the triploid form from 4 localities. Comparison of the enzymes of the triploid and the diploid digeneans showed 5 different patterns: diaphorase (EC 1.6.2.2), glutamic-oxaloacetic transaminase (EC 2.6.1.1),
hexokinase
(
EC 2.7.1.1
), leucylglycylglycine aminopeptidase (EC 3.4.1.3), and phosphoglucomutase (EC 2.7.5.1). On the basis of the numbers of bands and their patterns, all individuals of the triploid are probably heterozygous at each of these 5 loci and homozygous at the remaining 13 loci. The occurrence of fixed heterozygotes found in triploid populations cannot be easily explained by only a single mutation. It is suggested that the variability may have been introduced by hybridization with a different sub-species or a closely related species and may, thus, have been maintained since the time of the origin of triploids.
Parasitology 1985
Dec
PMID:Electrophoretic studies on enzymes of diploid and triploid Paragonimus westermani. 293 81
Isoenzyme patterns of adult Malaysian Schistosoma, S. mekongi and S. japonicum strains were analysed by isoelectric focusing (IEF) in polyacrylamide gel. Enzyme patterns obtained from Malaysian Schistosoma homogenates differed from those of S. mekongi and S. japonicum strains. Malaysian Schistosoma was found to differ from S. japonicum by 8 enzymes, namely phosphoglucomutase, phosphoglucoisomerase, malate dehydrogenase, acid phosphatase, hydroxy-butyrate dehydrogenase,
hexokinase
and alkaline phosphatase, and from S. mekongi by phosphoglucomutase, malate dehydrogenase, aldolase and alkaline phosphatase. These results and the distinct biology of the parasite suggest that Malaysian Schistosoma is a new species in the S. japonicum complex.
Southeast Asian J Trop Med Public Health 1985
Dec
PMID:Isoenzyme analyses of Malaysian Schistosoma, S. mekongi and S. japonicum by isoelectric focusing in polyacrylamide gel. 294 Jun 88
The intracellular distribution of the glycolytic enzymes
hexokinase
, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and the pyruvate kinase isoenzymes type M1 and type M2 within unfertilized hen eggs was studied. Most of glycolytic enzyme activities were found in the yolk fraction; 8-24% of total glycolytic enzyme activities were found in the vitelline membrane fraction. However, the specific activities of these enzymes in the vitelline membrane fraction are 19-72-fold higher (U/mg protein) and 45-178-fold more concentrated (U/g wet weight) than in the yolk fraction. The study of intracellular localization of pyruvate kinase isoenzymes shows that the blastodisc, latebra and vitelline membrane contain only pyruvate kinase type M2, whereas pyruvate kinase types M1 and M2 are found in the egg yolk. The exclusive occurrence of pyruvate kinase type M2 in the blastodisc is consistent with the concept that this isoenzyme is involved in the cell proliferation. The heterogeneous distribution of the glycolytic enzymes
hexokinase
, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase, and the heterogeneous localization of the pyruvate kinase isoenzymes types M1 and M2 indicate that glycolysis is distributed heterogeneously within the unfertilized hen egg cell.
Biochim Biophys Acta 1986
Dec
10
PMID:Demonstration of a heterogeneous distribution of glycolytic enzymes and of pyruvate kinase isoenzymes types M1 and M2 in unfertilized hen eggs. 294 22
1. The maximum activities of
hexokinase
, 6-phosphofructokinase and oxoglutarate dehydrogenase, together with capillary density and fibre composition, have been measured in muscle from male and female untrained, medium-trained and well trained individuals. 2. The activity of
hexokinase
was almost identical in muscle from the three groups, whereas that of 6-phosphofructokinase decreased and that of oxoglutarate dehydrogenase increased with increased training. Values of maximum rate of O2 uptake (VO2, max) were also measured and were 21% higher in medium-trained and 49% higher in well trained compared to untrained individuals, whereas oxoglutarate dehydrogenase activities were 39% and 90% higher respectively. 3. There was a good positive correlation between the activity of oxoglutarate dehydrogenase and the percentage of type I fibres but the correlation between VO2, max and oxoglutarate dehydrogenase activity was less good. Changes in the values of VO2, max represent the effects on the circulatory and respiratory system whereas those in oxoglutarate dehydrogenase represent local effects of endurance training.
J Physiol 1986
Dec
PMID:Maximum activities of key glycolytic and oxidative enzymes in human muscle from differently trained individuals. 295 91
Glycosomes, purified from trypomastigote forms of Trypanosoma brucei, contained all the enzymes necessary to convert glucose to alpha-glycerophosphate and 3-phosphoglycerate. The multienzyme reaction which produces 2 alpha-glycerophosphate, 2 ADP, and 2 NAD+ from 1 glucose, 2 ATP, and 2 NADH was studied spectrophotometrically. Intact glycosomes, suspended with 5.6 mM alpha-glycerophosphate and 2 mM ADP, produced ATP inside the glycosomes for glucose phosphorylation at a rate of 0.7 mumol/min/mg protein, so confirming the feasibility of producing ATP from alpha-glycerophosphate and ADP catalyzed by glycosomal glycerol kinase, and coupling this ATP production to the ATP-requiring stages of glycolysis. No evidence was found for direct channeling of the ATP generated by glycerol kinase and either
hexokinase
or phosphofructose kinase in glycosomal enzyme complexes cross-linked by dimethyl suberimidate treatment of intact glycosomes prior to solubilization of their membrane. Compartmentation of glycolytic intermediates, enzymes, and ATP inside isolated glycosomes was demonstrated by their inaccessibility to exogenous enzymes. We conclude that the compartmentation of the glycosome and the efficient production of ATP in the glycosome from whole cell concentrations of sn-glycerol 3-phosphate and ADP account for the observed whole cell production of equimolar glycerol from glucose with net ATP synthesis by T. brucei under anaerobic conditions.
J Biol Chem 1985
Dec
15
PMID:The role of compartmentation and glycerol kinase in the synthesis of ATP within the glycosome of Trypanosoma brucei. 299 27
The activity of some enzymes in a given metabolic pathway is modulated through multiple mechanisms, which operate in a simultaneous and coherent way to produce either stimulation or inhibition. The operation of these mechanisms is illustrated with several enzymes involved in glucose metabolism, by choosing examples from the presentations at the Symposium. Thus the reciprocal interactions of the regulatory mechanisms acting upon
hexokinase D
('glucokinase'), phosphofructokinase, fructose 1,6-bisphosphatase and pyruvate kinase were discussed, as well as their relationships with the induction of enzyme conformational changes. In addition, the effects of covalent interconversions on glutamine synthetase activity were briefly analyzed. An outstanding feature exhibited by all these enzymes is the display of a great number of elasticity coefficients, which are differential quotients measuring the dependence of enzymatic activity on each variable that modulates it. A general assumption is that these enzymes make an important contribution to the control of the metabolic flux in which they participate. The flux control, however, appears to be shared in different degrees by all the components of the system, and may be quantified through the differential quotient denominated control coefficient. Some of the problems that emerge in any attempt to estimate these coefficients in the living cells are discussed. The problems derive partly from the complex subcellular structure, the formation of functional compartments resulting from reversible association of the enzymes, one to another and to different cellular components, and the actual state of cell water. These problems make that the results obtained with purified and highly diluted enzymes in most enzymological studies should not be extrapolated directly to what happens in vivo, without a careful evaluation of each particular case. The regulatory role of enzyme activity of fructose 2,6-bisphosphate and its eventual participation as an intermediary in the hormonal control of glycolytic and gluconeogenic fluxes are emphasized. The regulation of yeast fructose 1,6-bisphosphate activity is discussed in relation to the eventual role of allosteric modulators and covalents interconversions as signals for the initiation of intracellular degradation of the enzyme during catabolic inactivation.
Arch Biol Med Exp 1985
Dec
PMID:[Concurrence of multiple and integrated mechanisms in the modulation of enzyme activities: significance for the regulation of metabolic fluxes]. 301 48
Malnourished patients without cancer have abnormal glucose metabolism, low activities of the key enzymes of glycolysis in muscle, and abnormal muscle fiber-type distribution. Malnutrition in cancer is also associated with altered glucose metabolism, and therefore muscle enzyme activities and fiber types were measured in 17 malnourished patients with gastrointestinal cancer (weight loss, 18.1% +/- 7.9 SD). These patients were matched with 17 depleted noncancer patients (weight loss, 22.8% +/- 10.25 SD) and 17 normal controls. Results of in vitro measurement of the maximal activity of phosphofructokinase (PFK),
hexokinase
(HK), and oxogluterate dehydrogenase (OGD) were similar in both undernourished groups and lower than that of normal controls. Both groups also had reduced Type II fiber size and number. The activity of fructose bisphosphatase (FBP) was significantly higher in cancer patients (0.62 mu ml min-1 g +/- 0.26 SD) than in noncancer patients (0.39 +/- 0.15), but similar to that in controls (0.65 +/- 0.29). As FBP is involved in substrate cycling, inappropriately high activity reflects an inability to adapt to malnutrition that could lead to high rates of cycling and wasteful energy expenditure at times of maximal activation of the cycle.
Cancer 1986
Dec
01
PMID:Abnormal muscle fructose bisphosphatase activity in malnourished cancer patients. 302 16
Nucleoside diphosphokinase (NDK) of human platelets has been purified by chromatography on Blue Sepharose CL-6B gel (purification factor of 950) and shown to be free of adenylate kinase, ATPase and adenylate cyclase. The molecular weight was 70,000 with subunits of 17,000. The pH optimum was 8.0 Km values for ATP and dTDP were determined in two ways using the pyruvate kinase-lactate dehydrogenase coupled enzyme assay. Values of 0.38 and 0.20 mM were obtained for ATP and 0.29 and 0.21 mM for dTDP. Km values for ADP (0.024 mM) and GTP (0.12 mM) were determined with the
hexokinase
-glucose-6-phosphate dehydrogenase coupled enzyme assay. These values are in agreement with those reported for NDK from other sources. Theophylline, which inhibits the NDK activity of intact platelets and platelet membrane preparations and inhibits the ADP-induced shape change of platelets, was shown to be a competitive inhibitor of both the free and phosphorylated forms of NDK with competitive inhibition constants (Kic) of 9.3 and 9.6 mM respectively. Papaverine, another cAMP phosphodiesterase inhibitor, which also inhibits the ADP-induced shape change of platelets, had no inhibitory effect on platelet NDK. It was concluded that the inhibitory effect of theophylline on the activity of the purified enzyme was due to the structural similarity between the methylxanthine and the adenine moiety of ADP.
Biochem Pharmacol 1986
Dec
15
PMID:Isolation and kinetic studies of nucleoside diphosphokinase from human platelets and effects of cAMP phosphodiesterase inhibitors. 302 50
Enzymes of the glycolytic pathway as well as some ancillary enzymes were studied in normal red cells parasitized with Plasmodium falciparum in culture at varying parasitemias as well as in isolated parasites. The levels of all enzymes except diphosphoglycerate mutase, glucose-6-phosphate dehydrogenase, and adenylate kinase were elevated. Extreme elevations of
hexokinase
, aldolase, enolase, pyruvate kinase, and adenosine deaminase concentrations were noted. In most cases, electrophoretically distinct bands of enzyme activity were also seen. These findings partly explain the previously noted 50- to 100-fold increase in glucose consumption of infected red cells and suggest that further knowledge of these parasite enzymes and their genetic basis may aid both in designing new chemotherapy and in understanding the evolution of these parasites.
Blood 1988
Dec
PMID:The enzymes of the glycolytic pathway in erythrocytes infected with Plasmodium falciparum malaria parasites. 305 30
Saccharomyces cerevisiae glucokinase (GLK) is the only described hexose-phosphorylating enzyme specific for aldo-hexoses. The gene was cloned by complementation of a triple mutant lacking all hexose-phosphorylating isoenzymes. Restriction sites were confirmed by genomic hybridization and GLK1 was mapped on chromosome III by ROFAGE, a method derived from the orthogonal field alteration gel electrophoresis. The mapping data were in agreement with previous genetic data. The open reading frame was established by two transcription start points in front of the initial ATG codon and by C-terminal beta-galactosidase fusions. The mRNA is 1.75 kb long and codes for 500 amino acid (aa) residues. Diversity of GLK from hexokinases PI and PII is very marked, with only 26 and 28% overall aa homology. A central core of about 350 aa shows 39% homology. No cross-hybridization could be observed by Southern hybridization. However, strong homologies were found over a range of 11 aa between glucokinase, yeast hexokinases (PI, PII) and rat
hexokinase
with 8 aa in common. These strongly conserved homologies give support to the view that this aa region corresponds to the binding site for glucose. Unlike all other hexose-phosphorylating enzymes, there is no proline residue indicating a conformational turn next to this glucokinase region. This finding may explain the failure of fructose phosphorylation. In both GLK and the hexokinases, a lysine residue is also conserved at aa position 110 which probably corresponds to the ATP-binding site. Additionally, a consensus sequence of 8 aa residues which is common for ATP-binding enzymes is conserved within the C-terminal part of GLK. The codon bias index for GLK1 is 0.25, which is very low compared with other glycolytic enzymes described so far. The gene is moderately expressed and constitutive on different carbon sources investigated. GLK1 null alleles had no detectable effects on sporulation and growth. Hence, a physiological role for GLK, which might explain its preservation, could not be detected under our laboratory test conditions.
Gene 1988
Dec
15
PMID:Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme. 307 53
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