Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Biopsies from m. quadriceps femoris from the operated leg of nine patients were taken before, and 6 weeks after, knee surgery. During the whole postoperative period the operated leg was immobilized with the knee in 40-50 degrees of flexion. Myoglobin (MYO) and the enzymes citrate synthase (CS), creatine kinase (CK) and its isozymes MB (CK-MB) and mitochondrial CK (CK-MIT), aspartate aminotransferase (ASAT), phosphofructokinase (PFK) and lactate dehydrogenase (LD) were determined on the biopsies. Citrate synthase, ASAT, CK, CK-MB, CK-MIT and LD activities were decreased (12-30%) after the postoperative leg immobilization period. Phosphofructokinase did not change, while MYO content was increased (16%). In conclusion, a different control of the synthesis of oxidative enzymes and MYO is suggested, as the induced changes following immobilization were in opposite directions. The function of the increased MYO content may be to facilitate the oxygen extraction.
 ...
PMID:Increase in myoglobin content and decrease in oxidative enzyme activities by leg muscle immobilization in man. 297 30

Although pyruvate carboxylase associated with both mitochondrial aspartate aminotransferase and malate dehydrogenase, it had a higher affinity for the amino-transferase. Furthermore, the aminotransferase enhanced dissociation of malate dehydrogenase from pyruvate carboxylase. Glutamate dehydrogenase did not associate with pyruvate carboxylase alone, but it apparently associated with the pyruvate carboxylase-aminotransferase complex, and malate dehydrogenase associated with the resulting ternary complex. Citrate synthase and other proteins tested did not associate with pyruvate carboxylase. However, citrate synthase associated with the pyruvate carboxylase-malate dehydrogenase complex. Apparently as a consequence of these heteroenzyme interactions, the rate of the pyruvate carboxylase reaction was slightly greater when coupled with malate dehydrogenase or both malate dehydrogenase and citrate synthase than when coupled with citrate synthase alone. In addition, in the presence of both coupling enzymes, the rate of conversion of pyruvate to citrate was higher than predicted on the basis of the Michaelis-Menten relationship of the two coupling enzymes. Therefore, binding of malate dehydrogenase to pyruvate carboxylase enhances pyruvate carboxylase activity. Association of citrate synthase with the malate dehydrogenase-pyruvate carboxylase binary complex does not alter activation of pyruvate carboxylase but results in citrate synthase being more reactive than free citrate synthase with oxalacetate.
 ...
PMID:Interactions between pyruvate carboxylase and other mitochondrial enzymes. 834 77

Two alpha-amylase-producing strains of Aspergillus oryzae, a wild-type strain and a recombinant containing additional copies of the alpha-amylase gene, were characterized with respect to enzyme activities, localization of enzymes to the mitochondria or cytosol, macromolecular composition, and metabolic fluxes through the central metabolism during glucose-limited chemostat cultivations. Citrate synthase and isocitrate dehydrogenase (NAD) activities were found only in the mitochondria, glucose-6-phosphate dehydrogenase and glutamate dehydrogenase (NADP) activities were found only in the cytosol, and isocitrate dehydrogenase (NADP), glutamate oxaloacetate transaminase, malate dehydrogenase, and glutamate dehydrogenase (NAD) activities were found in both the mitochondria and the cytosol. The measured biomass components and ash could account for 95% (wt/wt) of the biomass. The protein and RNA contents increased linearly with increasing specific growth rate, but the carbohydrate and chitin contents decreased. A metabolic model consisting of 69 fluxes and 59 intracellular metabolites was used to calculate the metabolic fluxes through the central metabolism at several specific growth rates, with ammonia or nitrate as the nitrogen source. The flux through the pentose phosphate pathway increased with increasing specific growth rate. The fluxes through the pentose phosphate pathway were 15 to 26% higher for the recombinant strain than for the wild-type strain.
 ...
PMID:Identification of enzymes and quantification of metabolic fluxes in the wild type and in a recombinant aspergillus oryzae strain 987 53