Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tetrahymena pyriformis Wh 14 was grown in Erlenmeyer flasks under continuous stirring at 30 degrees C for three days . After the culture had produced dry matter of about 100 mg HCB was added in acetone at a dose level of 0, 0.001, 0.1 and 1.0 ppm to the culture and incubated for another 7 days. At a dose level of 0.001 ppm the activity of delta-aminolevulinate dehydratase, hexokinase, and pyruvate kinase remained unaffected but was increased for glutamic-oxaloacetic transaminase, glutamic dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase while 0.1 ppm HCB increased the activity of all enzymes studied, the only exception being glutamic-pyruvic transaminase, the activity of which was depressed by HCB exposure. A concentration of 1.0 ppm HCB depressed the activity of most of the enzymes below control values with the exception of the two mitochondrial enzymes, MDH and ICDH, studied here.
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PMID:Effect of hexachlorobenzene (HCB) on the activity of some enzymes from Tetrahymena pyriformis. 10 53

1. In a group of 23 obese women the relations between some indicators of thyroid function (thyroxine-binding globuline--T4BG, triiodothyronine-binding globuline--T3BG, Achilles tendon reflex--ART) on the one hand and activities of enzymes of the energy metabolism (hexokinase--HK, triose phosphate dehydrogenase--TPDH, lactate dehydrogenase--LDH, glycerol-3-phosphate dehydrogenase--GPDH, citrate synthease--CS, malate dehydrogenase--MDH, hydroxyacyl--COA dehydrogenase) in the quadriceps femoris muscle on the other hand were investigated. 2. Correlations were found between T4BG and TPDH, LDH and GPDH activities, between T3BG and TPDH and GPDH activities and between the value of the Achilles tendon reflex and TPDH activity. Functionally these enzymes activities are associated with glycolysis and hydrogen transport from cytoplasmatic NADH2. No correlations were found between enzymes of the aerobic metabolism incl. enzymes of fatty acid oxidation and indicators of thyroid function. 3. The results indicate a relationship between thyroid function and enzymes involved in glycolysis and hydrogen transport from cytoplasmatic NADH2. They do not suggest, however, the unequivocal conclusion that in obese women with reduced thyroid function there is a generally reduced energy supplying metabolism in skeletal muscle.
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PMID:Obesity and thyroid function. 3. Relationship between some indicators of thyroid function and the energy metabolism of striated muscle in obese women. 41 51

1. In rat kidney cortex, outer and inner medulla the development of activities of seven enzymes was investigated during postnatal ontogeny (10, 20, 30, 60 and 90 days of age). The enzymes were selected in such a manner, as to characterize most of the main metabolic pathways of energy supplying metabolism: hexokinase (glucose phosphorylation, HK), glycerol-3-phosphate dehydrogenase (glycerolphosphate metabolism or shunt, GPDH), triose phosphate dehydrogenase (glycolytic carbohydrate breakdown, TPDH), lactate dehydrogenase (lactate metabolism, LDH), citrate synthase (tricarboxylic acid cycle, aerobic metabolism, CS), malate NAD dehydrogenase (tricarboxylic acid cycle, intra-extra mitochondrial hydrogen transport, MDH) and 3-hydroxyacyl-CoA-dehydrogenase (fatty acid catabolism, HOADH). 2. The renal cortex already differs metabolically from the medullar structures on the 10th day of life. It displays a high activity of aerobic breakdown of both fatty acids and carbohydrates. Its metabolic capacity further increases up to the 30th day of life. 3. The outer medullar structure is not grossly different from the inner medulla on the 10th day of life. Further it differentiates into a highly aerobic tissue mainly able to utilize carbohydrates. It can, however, to some extent, also utilize fatty acids aerobically and produce lactate from carbohydrates anaerobically. 4. The inner medullar structure is best equipped to utilize carbohydrates by anaerobic glycolysis, forming lactate. This feature is already pronounced on the 10th day of life, its capacity increases to some extent during postnatal development, being highest between the 10th and the 60th day of life.
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PMID:Postnatal changes of some enzymatic activities of energy supplying metabolism in the cortex, inner and outer medulla of the rat kidney. 644 14

In aggregates of nervous tissue, cultivated for 1--7 days at 0 degree C and 37 degrees C, respectively, the activities of seven enzymes of energy liberating metabolism were estimated, in order to evaluate their metabolic "profiles" and changes during cultivation. The enzymes used as markers of different pathways of energy liberation from substrates were: lactate dehydrogenase - LDH - (EC 1.1.1.27), triose-3-phosphate dehydrogenase - TPDH - (EC 1.2.1.12), glycerol-3-phosphate dehydrogenase - GPDH - (EC 1.1.1.8), hexokinase - HK - (EC 2.7.1.1.), malate:NAD dehydrogenase - MDH - (EC 1.1.1.37), citrate synthase - CS - (EC 4.1.3.7), and 3-hydroxyacetyl CoA dehydrogenase - HOADH - (EC 1.1.1.35). During the cultivation, some changes in the metabolic "profiles" were observed. Although some of these changes as well as the differences between the cultivation at 0 degree C and 37 degrees C, were statistically significant, they were not greater than the variations between different samples of any tissue taken at different times. They were not, therefore considered to be of major significance. However, all the aggregates exhibited "profiles" characteristic for the nervous tissue, with relatively very high activity of HK, high activity of MDH and CS (carbohydrate breakdown) and low activity of GPDH and HOADH (lipid catabolism).
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PMID:Enzyme activity pattern in developing mouse brain in situ in embryonic brain aggregated cells at 37 degrees C and 0 degree C. 661 8

The relative mobilities of six enzymes from the trophozoites of five axenically-cultured isolates of Giardia from human, cat, and guinea pig hosts were compared by starch and polyacrylamide gel electrophoresis. The six enzymes compared were malate dehydrogenase (NAD+) (MDH) (EC 1.1.1.37), malate dehydrogenase (decarboxylating) (ME) (EC 1.1.1.40), hexokinase (EC 2.7.1.1), 6-phosphogluconate dehydrogenase (EC 1.1.1.44), glucose-6-phosphate dehydrogenase (G6P) (EC 1.1.1.49), and alpha-glycerophosphate dehydrogenase (EC 1.1.1.8). The latter three enzymes have not been previously reported in Giardia. On the basis of zymogram patterns, the five Giardia isolates were divided into three zymodemes. Zymodeme I comprised human-1/England, human-1/Bethesda, and cat-1/Portland, Zymodeme II the guinea pig-1/Portland isolate, and Zymodeme III the human-1/Portland isolate. These zymodemes were further substantiated when several physical and kinetic properties of three of the enzymes, MDH, ME, and G6P, were examined. Our results, in which Giardia isolated from different mammalian hosts share multiple isoenzymes, question the validity of the practice of assigning Giardia species names on the basis of the animal host from which the protozoan was obtained.
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PMID:A comparison of isozymes of five axenic Giardia isolates. 667 61

Clones of 32 strains of Trichomonas vaginalis isolated from patients attending a venereal diseases clinic were compared among themselves and with authentic Pentatrichomonas hominis on the basis of their isoenzyme patterns for eight enzymes by thin-layer starch-gel electrophoresis. The enzymes examined were: glucose phosphate isomerase (GPI); phosphoglucomutase (PGM); malic enzyme (NADP+) (ME); hexokinase (HK); malate dehydrogenase (NAD+) (MDH); glucose-6-phosphate dehydrogenase (G6PD); aldolase (ALD); and lactate dehydrogenase (LDH). From the isoenzyme patterns of four enzymes (LDH, MDH, HK, and GPI) the strains of T vaginalis could be divided clearly into five groups. PGM showed differences in only one strain, while two other enzyme patterns (ME and ALD) were the same for all the strains of T vaginalis tested. All isolates were clearly distinguishable from P hominis. Although G6PD patterns were not sharp some differences were evident among T vaginalis strains.
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PMID:Isoenzyme characterisation of Trichomonas vaginalis. 698 Jun 85

A microassay method sensitive enough to analyze the enzyme activities in one oocyte was developed using enzymatic cycling for amplifying the reaction product to 10,000 fold. An oil-well technique was applied in the assay for achieving the reaction in the medium as small as 1.0 to 5.0 microliter. Immature Wistar rats were superovulated by PMS-hCG administration. Oocytes were collected by the puncture of the follicle and the flushing of the tube. They were freeze-dried after washing to remove cumulus cells. The dry weight was about 50ng on a quartz fiber fishpole balance. The activity of hexokinase was 1.75 +/- 0.14 picomol/oocyte/hr corresponding to one-tenth of the ovarian homogenate as control, indicating low capacity of glucose utilization in the oocyte. The activities of G6PD, LDH, and MDH were 8.41 +/- 0.34, 35.7 +/- 2.89. 11.1 +/- 2.5 picomol/oocyte/min, respectively. High activity of G6PD suggests the pentose phosphate shunt concerned with steroidogenesis is active in the oocyte. HCG increased the activities of hexokinase and MDH and decreased that of G6PD. The activity of LDH remained unchanged.
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PMID:[Study of energy metabolism in the oocyte by cycling method]. 717 80

Changes in the activity of muscle enzymes of energy metabolism were studied in two groups of skiers (A, B) with a different sports performance (triosephosphate dehydrogenase-TPDH, lactate dehydrogenase-LDH, glycerol-3-phosphate dehydrogenase-GPDH, hexokinase-HK, malate dehydrogenase-MDH, citrate synthase-CS, hydroxyacyl,CoA dehydrogenase-HOADH). 1. In a group of ski-runners (A) significantly higher activities of CS, MDH, HOADH in the preparatory period (October) and also at the end of the competition period (March) were found in athletes with higher sports performance. 2. Significantly lower activities of LDH, GPDH, MDH, CS, HOADH were found in downhill skiers (group B). 3. Some significant correlations were established, both between the activities of individual enzymes (TPDH, GPDH, HK, CS, HOADH) and between the enzymes and indicators of functional capacity (MDH, CS, HOADH, VO2max, HRmax, O2-pulse max, body fat, laboratory performance).
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PMID:Enzyme activity patterns of energy metabolism in skiers of different performance levels (M. quadriceps femoris). 720 Aug 74

Ultraviolet (UV) radiation is one of the major risk factors of cataract (loss of eye-lens transparency). The influence of UVB radiation (300 nm; 100 microW cm-2) on the activity and apparent kinetic constants (Km and Vmax) of rat lens hexokinase (HK;EC 2.7.1.1), phosphofructokinase (PFK; EC 2.7.1.11), isocitrate dehydrogenase (ICDH; EC 1.1.1.41) and malate dehydrogenase (MDH; EC 1.1.1.37) of energy metabolism has been investigated by irradiating the lens homogenate of three- and 12-month-old rats. In the three-month-old group specific activities of HK and PFK are reduced by 56 and 43%, respectively, and there is no change in ICDH and MDH activities after a 24 h exposure. On the other hand, in the 12-month-old group the decreases are 72, 71, 24 and 16% for HK, PFK, ICDH and MDH, respectively. UVB irradiation increases the apparent Km of HK and PFK (in both age groups), whereas the Km of ICDH and MDH is not altered. While the decrease in Vmax of these enzymes due to UVB exposure is only marginal in three-month-old rats, it is more pronounced (significant) in 12-month-old rats. A similar decrease in enzyme activities of HK and PFK is also observed upon UVB exposure of the intact rat lens. The photoinduced changes in energy metabolism may in turn have a bearing on lens transparency, particularly at an older age.
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PMID:UVB irradiation alters the activities and kinetic properties of the enzymes of energy metabolism in rat lens during aging. 949 95

The purpose of the present study was to compare the ontogenetic development of the activity of myocardial energy-supplying enzymes in two mammalian species, differing significantly in their level of maturation at birth. The animals were investigated during the late prenatal period and 2, 7, 14, 21, 25, 30, 63, 120 and 730 days after birth in the rat and 2, 21, 84 and 175 days in the guinea-pig. The following enzymes were assayed in the right and left ventricular myocardium: lactate dehydrogenase (LDH, lactate uptake and/or formation), triose phosphate dehydrogenase (TPDH, carbohydrate metabolism), glycerol phosphate dehydrogenase (GPDH, glycerol-P shuttle)), hexokinase (HK, glucose phosphorylation), malate dehydrogenase (MDH, tricarboxylic cycle), citrate synthase (CS, tricarboxylic cycle) and hydroxyacyl-CoA dehydrogenase (HOADH, fatty acid breakdown). The rat heart, highly immature at birth, exhibits three different developmental patterns of energy-supplying enzymes, identical in both ventricles: (i) two mitochondrial enzymes of aerobic metabolism (CS, HOADH) and GPDH have a relatively low activity at the end of prenatal life; thereafter their activity steadily increases, approaching the adult levels between the 3rd and 4th postnatal weeks. A significant decrease was observed between the 4th and 24th months. (ii) MDH and LDH: prenatal values were significantly higher as compared with the 2nd postnatal day; after this period the activities increased up to adulthood (4 months) and decreased during senescence. (iii) The activities of HK and TPDH are characterized by only moderate changes during development. HK differs from all other enzymes by the highest prenatal values, which exceed even adult values. In contradiction to the rat heart, the developmental differences in more mature guinea-pig heart were significantly less pronounced. The only ontogenetic differences observed were the lower activities of enzymes connected with aerobic metabolism at the end of the prenatal period. Our results point to possible differences in the development of adaptive metabolic pathways in animals with different levels of maturation at birth.
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PMID:Ontogenetic development of energy-supplying enzymes in rat and guinea-pig heart. 1152 34


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