Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eleven soluble enzymes in the supernatant of bloodstream Trypanosoma brucei were compared for electrophoretic mobility and activity with those of T. brucei cultures grown in 3 different media. All bands of each enzyme found in the bloodstream form were also present in the cultured material, but extra bands of malate dehydrogenase (MDH) (EC 1.1.1.37), aspartate aminotransferase (ASAT) (EC 2.6.1.1), and in 2 to 6 cultures of isocitrate dehydrogenase (ICD) (EC 1.1.1.42) were present in culture forms but not in bloodstream forms. An interfering enzyme, peculiar to cultured T. brucei, which reacted with 2-oxoglutarate and possibly a trace amount of ammonium ions, ran with the fast-moving ASAT bands. Threonine dehydrogenase activity, high in cultured trypanosomes irrespective of the medium used but low in bloodstream trypanosomes, was markedly lower in Trypanosoma evansi and a much passaged T. brucei 8/18. Glucosephosphate isomerase activity on the other hand was high in bloodstream and low in cultured trypanosomes. Glutamate dehydrogenase activity was too low to record reliably in bloodstream trypanosomes, but could be clearly detected in cultured forms. As the differences point to some changes in gene expression between the two forms, culture material is likely to replace trypanosomes from living animals for electrophoretic characterization only when considerable comparative work has been done.
Mol Biochem Parasitol 1980 Oct
PMID:The electrophoretic mobilities and activities of eleven enzymes of bloodstream and culture forms of Trypanosoma brucei compared. 645 Aug 96

The usefulness of measuring serum-conjugated bile acid concentrations by radioimmunoassay in colchicine-modified carbon tetrachloride-induced liver lesions in rats was assessed by comparing the concentrations with the results of some routinely employed liver function tests such as serum aspartate transaminase, alanine transaminase, alkaline phosphatase, and serum total protein. The serum cholylglycine levels were significantly (P less than 0.003) raised along with the serum aspartate transaminase (P less than 0.01) and alanine transaminase (P less than 0.01) activity levels in the carbon tetrachloride-treated group of rats when compared with the group treated with carbon tetrachloride plus colchicine. Colchicine prevented the increase in serum cholylglycine, aspartate transaminase, alanine transaminase, and alkaline phosphatase induced by carbon tetrachloride but had no effect on serum total protein levels. This study suggests that radioimmunoassay of serum cholyglycine is a sensitive and specific indicator of liver injury and it is a useful tool in monitoring the treatment provided.
Exp Mol Pathol 1984 Dec
PMID:Serum bile acid in the evaluation of colchicine treatment of carbon tetrachloride-induced liver injury. 651 May 12

The enzyme, aspartate aminotransferase, is a dimer consisting of two identical subunits which contain overlapping subunit regions ( Eichele , G., Ford, G.C., Glor , M., Jansonius , J.N., Mavrides , C., and Christen , P. (1979) J. Mol. Biol. 133, 161-180), suggesting the possibility of subunit interactions. The structurally similar cytosolic isozyme exhibits noncooperative binding of pyridoxal 5'-phosphate ( Boettcher , M., and Martinez -Carrion, M. (1975) Biochemistry 14, 4528-4531; Relimpio , A., Iriarte , A., Chlebowski , J.F., and Martinez -Carrion, M. (1981) J. Biol. Chem. 256, 4478-4488) in which the apoenzyme/holoenzyme hybrid dimer shows a distinctive thermal stability. Using a nonequilibrium isoelectric focusing technique, it can be shown that mitochondrial aspartate aminotransferase also binds cofactor in a noncooperative random fashion. However, differential scanning calorimetry (DSC) thermograms show different characteristics from the cytosolic form. These differences are interpreted in terms of unique subunit interactions in this isozyme. Heating to the various DSC transition temperatures shows that the anomalous DSC thermograms in partially coenzyme-saturated apoenzyme preparations are due to a selective dissociation of apoenzyme subunits into monomers which are irreversibly denatured. The remaining holoenzyme monomers reassociate and form stable holoenzyme dimers. The net result is retention of the initial concentration of holoenzyme subunits present in any given mixture. Random occupancy of active sites and similar electrophoretic and DSC patterns upon heating of partially saturated apoenzyme preparations is observed whether the coenzyme, pyridoxal phosphate or pyridoxamine phosphate alone, or borohydride-reduced Schiff's bases of coenzyme-substrate analogue derivatives are used as active site directed ligands. The latter resemble covalent enzyme-substrate intermediates.
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PMID:Coenzyme active site occupancy as an indicator of independence of the subunits of mitochondrial aspartate aminotransferase. 672 80

We have determined the nucleotide sequence at the distal end of the heat-labile enterotoxin subunit A (LT-A) gene (toxA) originating from human enterotoxigenic Escherichia coli. The sequenced region covers the entire LT-A2 region and a part of the LT-A1 region. In confirming our previous prediction based on product analysis of clones toxA regions, the data suggest the overlapping of the distal end (5'-TTA TGA) of toxA with the proximal end (5'-ATG AAT) of the LT subunit B gene (toxB), in the sequences 5'-TTATGAAT. Some additional characteristics of the LT operon as well as of the products are discussed.
Mol Gen Genet 1982
PMID:Overlapping genes in the heat-labile enterotoxin operon originating from Escherichia coli human strain. 675 77

Native mitochondrial aspartate aminotransferase (AATase) is cleaved selectively by trypsin at the peptide bonds after Arg 26 or after Lys 31 yielding two shortened enzyme derivatives, AATase 27-410, and AATase 32-410. Recent x-ray crystallographic determination of the spatial structure of AATase has shown that the NH2-terminal segments of the two polypeptide chains of this dimeric enzyme pass in front of the active site clefts and form two separate junctions with the neighboring subunit which are not contiguous with the main subunit interface (Eichele, G., Ford, G. C., Glor, M., Jansonius, J. N., Mavrides, C., and Christen, P. (1979) J. Mol. Biol. 133, 161-180). The peptide bonds cleaved by trypsin are situated in the following stretch of the polypeptide chain which runs in exposed position on the surface of the subunit. The split-off peptide is lost during gel filtration. The molecular activity of AATase 27/32-410 (a mixture of about equal amounts of the two not readily separable derivatives) is about 3% of that of the native enzyme. In contrast, the K'm values for aspartate and 2-oxoglutarate are unchanged, indicating an unaltered geometry of the substrate binding site. A substantially diminished syncatalytic response of the reactivity of Cys 166 toward 5,5'-dithiobis-(2-nitrobenzoate) suggests that the decrease in catalytic activity is due to an interference with the syncatalytic conformational dynamics observed previously in AATase (Gehring, H., and Christen, P. (1978) J. Biol. Chem. 253, 3158-3163). Consonant with a role of the NH2-terminal segment in propagating the syncatalytic conformational rearrangements the rate of the tryptic cleavage is retarded 4-fold in the presence of the transaminating substrate pair aspartate and oxalacetate.
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PMID:Mitochondrial aspartate aminotransferase 27/32-410. Partially active enzyme derivative produced by limited proteolytic cleavage of native enzyme. 743 Jan 25

Erythrocyte aspartate aminotransferase (AST) and alanine aminotransferase (ALT) activities are often used as indices of vitamin B-6 nutritional status; however, results using a mixed population of erythrocytes can be quite variable. Erythrocytes from two strains of mice (Mus domesticus), A/Ibg and DBA/Ibg, were separated according to age by centrifugation through discontinuous Percoll density gradients into three fractions: top (least dense, youngest), middle and bottom (most dense, oldest). A sufficient yield of age-fractionated erythrocytes was obtained from a single mouse for all of the enzyme measurements. The activities of AST, ALT and three age-marker enzymes, pyruvate kinase, acetylcholinesterase and hexokinase, were found to be significantly higher in the youngest cell fractions, and declined in the older, more dense fractions. A mice had significantly lower AST and ALT activities in the age separated fractions than did DBA mice. The measurement of enzyme activities in low density, young cells may be especially useful in studies involving conditions in which the proportion of young erythrocytes may be elevated with respect to the entire erythrocyte mass.
Comp Biochem Physiol B Biochem Mol Biol
PMID:Aminotransferase activities in mouse, Mus domesticus, erythrocytes separated according to age. 755 57

The activity and some kinetic parameters of the key enzymes of the glycolysis, the gluconeogenesis and the amino acid catabolism from the liver of male and female mink have been determined and compared to the corresponding activities from rat and cat. The activities of glucose-6-phosphatase and pyruvate kinase are dependent on sex, both being higher in females. Except for pyruvate carboxylase the glycolytic and the gluconeogenic enzyme activities of the mink are higher than those of rat and cat; especially the activities of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase are markedly higher. The activities of glutamate dehydrogenase and glutamate oxaloacetate transaminase are smaller than the corresponding activities of rat but higher than those of cat. The results suggest that mink has a high capacity for gluconeogenesis compared to rat.
Comp Biochem Physiol B Biochem Mol Biol 1995 Sep
PMID:Activities of carbohydrate and amino acid metabolizing enzymes from liver of mink (Mustela vison) and preliminary observations on steady state kinetics of the enzymes. 758 47

Five aspartate aminotransferase (EC 2.6.1.1; AAT) isozymes were identified in soybean seedling extracts and designated AAT1 to AAT5 based on their rate of migration on non-denaturing electrophoretic gels. AAT1 was detected only in extracts of cotyledons from dark-grown seedlings. AAT3 and AAT4 were detected in crude extracts of leaves and in cotyledons of seedlings grown in the light. AAT2 and AAT5 were detected in all tissues examined. A soybean leaf cDNA clone, pSAT17, was identified by hybridization to a carrot AAT cDNA clone at low stringency. pSAT17 had an open reading frame which could encode a 50,581 Da protein. Alignment of the deduced amino acid sequence from the pSAT17 open reading frame with mature AAT protein sequences from rat disclosed a 60 amino acid N-terminal extension in the pSAT17 protein. This extension had characteristics of a plastid transit peptide. A plasmid, pEXAT17, was constructed which encoded the mature protein lacking the putative chloroplast transit polypeptide. Transformed Escherichia coli expressed a functional soybean AAT isozyme, which comigrated with the soybean AAT5 isozyme during agarose gel electrophoresis. Differential sucrose gradient sedimentation of soybean extracts indicated that AAT5 specifically cofractionated with chloroplasts. Antibodies raised against the pEXAT17-encoded AAT protein specifically reacted with the AAT5 isozyme of soybean and not with any of the other isozymes, indicating that the soybean cDNA clone, pSAT17, encodes the chloroplast isozyme, AAT5.
Plant Mol Biol 1993 Mar
PMID:Isolation and characterization of a soybean cDNA clone encoding the plastid form of aspartate aminotransferase. 768 17

A 3 kb genomic fragment containing the nusG gene of Streptomyces coelicolor A3(2) was identified, cloned and sequenced. Sequence analysis revealed 3 complete and 2 truncated open reading frames (ORFs): truncated ORFU (similar to a Bacillus gene encoding a thermostable aspartate aminotransferase)-secE (94 amino acids; 79.0% similarity to Escherichia coli SecE)-nusG (300 amino acids; 73.3% similarity to E. coli NusG)-rplK (144 amino acids; 88.5% similarity to E. coli ribosomal subunit L11)-truncated rplA (similar to E. coli ribosomal subunit L1). The gene organization secE-nusG-rplKA exactly matches that in E. coli. Transcriptional analyses by the primer extension method revealed one transcriptional start site each for secE and nusG, and two sites for rplK. The presence of promoters was also confirmed with the aid of a promoter-probe vector.
Mol Gen Genet 1995 Apr 10
PMID:Cloning, nucleotide sequence, and transcriptional analysis of the nusG gene of Streptomyces coelicolor A3(2), which encodes a putative transcriptional antiterminator. 771 99

Human placental cytoplasmic aspartate transaminase was purified 404-fold by heat treatment, ammonium sulfate fractionation, dialysis and DEAE-Sephadex chromatography. The pH optimum of the enzyme was 6.8 in either phosphate or cacodylate buffer. The Km values of alpha-ketoglutarate and L-aspartate were 2.06 and 22.5 mM, respectively. A 78% inhibition of the enzyme was noted at 4 mM concentration of maleate which inhibited the enzyme upon competing with alpha-ketoglutarate with a Ki value of 1.72 mM. The kinetic properties of this enzyme are compared with those of the enzyme from various mammalian and other sources. The data are discussed in terms of the probable effectiveness of this enzyme in catabolizing L-aspartate in placenta especially after the consumption of a high protein diet by the pregnant mother.
Comp Biochem Physiol B Biochem Mol Biol 1995 Feb
PMID:Partial purification and kinetic properties of human placental cytosolic aspartate transaminase. 771 46


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