Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glycosomes and mitochondrial vesicles from cultured promastigotes of Leishmania mexicana mexicana have been separated using isopycnic centrifugation on linear sucrose gradients. Hexokinase (EC 2.7.1.2), glucose phosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) were recovered largely in association with glycosomes (density; 1.215 g/ml). Phosphoglycerate kinase (EC 2.7.2.3) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) had some small glycosomal activity, but were mostly recovered in the soluble fractions. Malate dehydrogenase (EC 1.1.1.37) showed a broad peak corresponding to that of the mitochondrial marker oligomycin-sensitive ATPase (EC 3.6.1.4) (density; 1.190 g/ml). Glutamate dehydrogenase (EC 1.4.1.3) and alanine aminotransferase (EC 2.6.1.2) both showed small mitochondrial peaks, but most of the activities were recovered elsewhere on the gradient and in the soluble fractions. The subcellular location of enzymes in L.m. mexicana amastigotes was investigated by following the release of soluble enzymes from digitonin-treated amastigotes. This revealed distinct cytosolic, mitochondrial, and glycosomal compartments. The findings give an insight into the organization and control of L.m. mexicana promastigote and amastigote energy metabolism.
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PMID:Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. 315 38

Crocodilians such as caimans and alligators are uricotelic and ammoniotelic animals. They are carnivorous but they excrete ammonium ions in an alkaline urine. The metabolic organization of the kidney of the Mississippi alligator was studied by measuring the renal metabolite profile, the activities of enzymes, and the behavior of kidney tubules in vitro. The liver and tail muscle were also studied. Both awake and anesthetized animals were in a state of low plasma bicarbonate and low blood pH with high plasma lactate concentration. This did not prevent the excretion of an alkaline urine (pH 7.76). alpha-Ketoglutarate was low in all three tissues and lactate was high. Glutamate concentration and glutamate dehydrogenase activity were highest in the kidney with a low equilibrium constant for alanine aminotransferase (KGPT). Glutaminase I was found only in the kidney. It could not be detected in liver or muscle. Glutamine synthetase was found only in the liver. Phosphoenolpyruvate carboxykinase (PEPCK) was present in both liver and kidney. Alanine aminotransferase and malic enzyme showed high activity in the kidney but were inconspicuous in liver and muscle. Malate dehydrogenase and lactate dehydrogenase were present in all three tissues. Renal tubules incubated with glutamine and alanine were ammoniagenic and gluconeogenic. Lactate was gluconeogenic. Enzyme activities were measured at both 30 and 37 degrees C. The studies on renal tubules were also performed at these two temperatures. Temperature had little effect on the data including acid-base values in the blood. Our findings demonstrate that the kidney of the alligator is perfectly equipped for various metabolic functions and especially for ammoniagenesis and gluconeogenesis.
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PMID:Metabolic machinery of the alligator kidney. 649 95

The present study was designed to test if both the intensity and duration of the 45-min Square-Wave Endurance Exercise Test (SWEET) would produce changes in serum enzyme activities. Nine men, four sedentary (S) and five athletes (A), performed VO2 max and SWEET, at their Maximal Intensity of Endurance (MIE45) as defined by maximal heart rate and the impossibility of maintaining MIE 45 + 5% for 45 min. Arterial blood was sampled at rest (R), exercise (Ex) (45th min) and during recovery (15th min) for measurements of levels of Haemoglobin (Hb), Haematocrit (Hct), pH and seven serum enzymes: Creatine kinase (CPK), Hexose-phosphate isomerase (PHI), Aldolase (ALD), Lactate dehydrogenase (LDH), Malate dehydrogenase (MDH), Aspartate amino-transferase (ASAT or GOT), and Alanine aminotransferase (ALAT or GPT). Five enzymes increased significantly during exercise (MIE45), the delta % (Ex - R/R) increases were as follows: PHI (72%), MDH (28%), LDH (21%), CPK (17%), and GOT (13.5%), whilst only a 10% increase was observed for Hct and Hb and there was no significant change in the arterial pH. There was no correlation between the delta % of Hb, Hct, pH, and the results for the enzymes. Thus, it does not seem that haemoconcentration and arterial blood acidosis which occur during exercise are only at the origin of the observed increases in enzymes. A difference between "sedentary" and "athletes" subjects was found at rest and exercise (delta % = A - S/S) for CPK (R = 222%; Ex = 235%), GOT (R = 90%; Ex = 75%) and ALD (R = 99%; Ex = 54%). These results suggest that the MIE45, by measured increases in enzymatic activity, seems to require great muscular effort.
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PMID:Serum enzyme variations in men during an exhaustive "square-wave" endurance exercise test. 653 38

Heparin and quercetin induce capacitation in spermatozoa through membrane receptor binding and inhibition of Ca-ATPase of the plasma membrane, respectively. Although capacitation is energy intensive, ammonia from amino acid metabolism can inhibit respiration and Krebs cycle activity. The objective was to determine activities of key enzymes in bull spermatozoa that contribute to the redox state and supply energy for capacitation. Malate dehydrogenase (MDH-NAD(+)), alanine and aspartate aminotransferases (ALT, AST), and lactate dehydrogenase-X (LDH-X) were measured spectrophotometrically (340 nm); mean (+/-S.D.) activities in control spermatozoa were 7.65+/-1.67, 0.45+/-0.05 and 0.74+/-0.14x10(-2)U/10(8) spermatozoa for MDH-NAD(+), ALT and AST, respectively, and were 2.83+/-0.66U/10(8) spermatozoa for LDH-X. Heparin decreased (P<0.05) activities of MDH-NAD(+), ALT, AST and LDH-X (78, 53, 66 and 66% of control levels, respectively); we inferred that amino acid catabolism was decreased. Quercetin decreased (P<0.05) activities of MDH-NAD(+) and ALT (60 and 49% of control levels), but activities of AST and LDH-X were not significantly different from controls; apparently maintenance of LDH-X activity supplied pyruvate for cellular metabolism. The proportion of capacitated spermatozoa in controls (8.5+/-1.73%) was substantially increased (P<0.05) by treatment with either heparin (36.2+/-4.5%) or quercetin (32.8+/-4.7%), there was no significant difference among groups for acrosomal integrity and sperm viability. In conclusion, heparin- or quercetin-induced capacitation affected different metabolic pathways that modulated the redox state and oxidative metabolism in cryopreserved bovine spermatozoa.
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PMID:Heparin and quercitin generate differential metabolic pathways that involve aminotransferases and LDH-X dehydrogenase in cryopreserved bovine spermatozoa. 1708 43