Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.1 (aspartate aminotransferase)
 21,665 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The data of studies in the monoaminoxidase, nuclease and transaminase activity in fractions of mitochondria and nuclei of the human fetus brain in the process of the fetus development evidence for the changes in the activity depending on the morphological and functional maturation of the organ during the antenatal ontogenesis. The monoaminoxidase activity increases by the time of birth. By the 40th week of development the activity of glutamic-aspartic transaminase increases as well. The activity of glutamic-alanine transaminase changes insignificantly. A considerable decrease in the activity of DNase and RNase in the mentioned fractions is observed by the time of the fetus birth. The maximal activity of these enzymes is observed in the first half of the fetus intrauterine development.
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PMID:[Formation of some enzymic systems in the human fetal brain during development]. 66 28

Lysosomal degradation of intracellular proteins during serum withdrawal is stimulated by a member of the 70-kDa heat shock protein (hsp70) family (Chiang, H.-L., Terlecky, S. R., Plant, C. P., and Dice, J. F. (1989) Science 246, 382-385). This hsp70, isolated by affinity chromatography with RNase S-peptide-Sepharose, is referred to as the 73-kDa peptide recognition protein (prp73). We now report that prp73 binds to several proteins and peptides whose degradative rates are increased during serum withdrawal. prp73 also binds to the pentapeptide, KFERQ, and more weakly to most modified RNase S-peptide derivatives with a single amino acid substitution within the KFERQ sequence. Taken together, these results suggest that prp73 binds to a variety of proteins at peptide regions biochemically related to KFERQ. Three lines of evidence indicate that prp73 is the heat shock cognate protein of 73 kDa (hsc73): (a) among five hsp70s tested, hsc73 binds to RNase S-peptide most avidly, (b) both prp73 and hsc73 also bind to RNase A and aspartate aminotransferase but not to ovalbumin, lysozyme, or ubiquitin, and (c) both prp73 and hsc73 promote uptake and degradation of [3H] RNase S-peptide by lysosomes in vitro, while three other hsp70s are without activity in this assay.
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PMID:Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. 157 55

The activities of alanine aminotransferase (ES 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1) and monoaminoxidase (EC 1.4.3.4) in the liver nuclei and mitochondria of human fes rises gradually beginning from the early periods of the antenatal development till birth and reaches the highest value in the last month of the fetus intra-uterine life. The monoaminoxidase activity is found in the liver nuclei of 21-32-week human feti. The activity of RNase (EC 2.7.7.16) and DNase (EC 3.1.4.5) in the liver nuclei is 10 and 15 times as low, respectively, by the 40th week of development, and 1.5 times as low in mitochondria.
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PMID:[Comparative characteristics of the activity of enzyme systems for nitrogen metabolism in the liver of human fetuses during embryogenesis]. 713 1

During differentiation of mouse 3T3-L1 fibroblasts to an adipocyte phenotype, the mitochondrial isoform of aspartate aminotransferase accumulates on the plasma membrane. The determination of whether this reflects translation of an alternatively spliced message lacking the mitochondrial leader sequence required cloning of the enzyme's uncommon a allele, for which these cells are homozygous. The 1.4-kb cDNA sequence of the a allele was obtained from oligo-dT-primed reverse-transcriptase PCR products amplified from FVB mouse RNA. It differed from the b allele at only 2 bp and one amino acid. By contrast, gene-specific primers generated an additional 1.4-kb fragment that differed from the b allele by approximately 1% of nucleotides, encoding four amino acid substitutions. This sequence proved to represent a recently diverged processed pseudogene. The presence of such pseudogenes can complicate interpretation of expressed-sequence-tag data and single-nucleotide-polymorphism genotyping studies. Using probes derived from the a allele, RNase protection analyses indicated that only a single message for the enzyme was present in 3T3-L1 fibroblasts and adipocytes, despite differences in subcellular protein distribution.
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PMID:Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA. 1064 97

Allatostatins are important regulatory neuropeptides which are widely distributed in invertebrates and execute their functions through either neural or humoral routes. However, the regulatory mechanism of the gene expression is unclear. In this paper, we report a naturally occurring antisense transcript, named as asMacro-AST A, of the crustacean FGLamide allatostatin gene (Macro-AST A) from the prawn, Macrobrachium rosenbergii. The asMacro-AST A contains an 843-bp sequence fully complementary to the 3' end of the Macro-AST A. To our knowledge, this is the first report of a natural antisense transcript in crustacean and the first endogenous antisense transcript of all identified allatostatin genes. Northern blotting analysis demonstrated that the gene was expressed in the thoracic ganglia where the sense gene was also expressed. Furthermore, we have detected a RNA-RNA duplex between the sense-antisense complementary region by using RNase protection analysis and RT-PCR. These results suggest that the antisense gene may play a role in the regulation of Macro-AST A gene expression.
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PMID:Naturally occurring antisense RNA of allatostatin gene in the prawn, Macrobrachium rosenbergii. 1705 61

Alfalfa (Medicago sativa, Siwa 1) seeds were subjected to drought stress during germination by using polyethylene glycol (PEG 4000) for studying the changes in some enzyme activities involved in nitrogen metabolism and the content of nitrogenous compounds during the first four days of growth after putrescine (Put) treatment. Decreasing the external water potential reduced activities of glutamate-pyruvate transferase (GPT), glutamate-oxaloacetate transferase (GOT) and RNase. Some free amino acids such as proline and glycine increased, while alanine and aspartic acid decreased. Nucleic acids content also decreased. Polyamines e.g., spermidine (Spd) and spermine (Spm) increased at the water potential -0.4 MPa. Put treatment increased activities of GOT, GPT and RNase. Furthermore, Put treatment increased nucleic acids content and the endogenous polyamines under drought stress. Drought stress was imposed during seedling stage by decreasing soil moisture content. GOT, GPT and RNase activities increased in leaves of alfalfa seedlings under drought stress. Soluble nitrogenous compounds accumulated under drought stress, while nucleic acids content decreased. Except glutamic acid, all free amino acids detected increased under drought stress. Put treatment decreased activities of GOT, GPT and RNase, as well as reduced the accumulation of the total soluble nitrogenous compounds, but increased DNA, RNA and protein contents.
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PMID:Alterations in nitrogen metabolites after putrescine treatment in alfalfa under drought stress. 1906 67