Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.44 (AGT)
 770 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It was found in our previous study (Oda et al., 1990. J. Biol. Chem. 265: 7513-7519) that in the rat two mRNAs encoding mitochondrial and peroxisomal serine:pyruvate aminotransferase (SPT/AGT) are formed from a single SPT/AGT gene through alternative transcription initiation in exon 1. In an attempt to analyze the mechanisms underlying this unique phenomenon, we have isolated genomic clones harboring the entire rat SPT/AGT gene. In the present study, the location of the rat SPT/AGT gene was determined to be in the q34-q36 region of chromosome 9 by fluorescence in situ hybridization. Southern blot analysis of rat genomic DNA revealed an allelic BamHI restriction fragment length polymorphism among three different inbred rat strains. These results indicated that a single copy SPT/AGT gene is located on chromosome 9q34-q36 in the rat genome. This locus has been assigned the gene symbol Spat.
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PMID:A single serine:pyruvate aminotransferase gene on rat chromosome 9q34-q36. 163 96

A patient with primary hyperoxaluria type 1 (hepatic peroxisomal alanine:glyoxylate aminotransferase [EC 2.6.1.44] deficiency) was successfully treated by combined hepatic and renal transplantation. The metabolic lesion was corrected by replacement of the deficient hepatic enzyme activity.
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PMID:Successful treatment of primary hyperoxaluria type I by combined hepatic and renal transplantation. 288 76

The subcellular distribution of asparagine:oxo-acid aminotransferase (EC 2.6.1.14) in rat liver was examined by centrifugation in a sucrose density gradient. About 30% of the homogenate activity after the removal of the nuclear fraction was recovered in the peroxisomes, about 56% in the mitochondria, and the remainder in the soluble fraction from broken peroxisomes. The mitochondrial asparagine aminotransferase had identical immunological properties with the peroxisomal one. Glucagon injection to rats resulted in the increase of its activity in the mitochondria but not in the peroxisomes. Immunological evidence was obtained that the enzyme was identical with alanine:glyoxylate aminotransferase 1 (EC 2.6.1.44) which had been reported to be identical with serine:pyruvate aminotransferase (EC 2.6.1.51) (Noguchi, T. (1987) in Peroxisomes in Biology and Medicine (Fahimi, H. D., and Sies, H., eds) pp. 234-243, Springer-Verlag, Heidelberg). The same results as described above were obtained with mouse liver. All of alanine:glyoxylate aminotransferase 1 in livers of mammals other than rodents, which cross-react with the antibody against rat liver alanine:glyoxylate aminotransferase 1, had no asparagine aminotransferase activity.
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PMID:Identification of mammalian aminotransferases utilizing glyoxylate or pyruvate as amino acceptor. Peroxisomal and mitochondrial asparagine aminotransferase. 312 7

We have reported the isolation of genomic clones encoding serine:pyruvate aminotransferase (SPT; also named alanine:glyoxylate aminotransferase, AGT) (T. Oda, T. Funai, and A. Ichiyama, 1990, J. Biol. Chem. 265: 7513-7519). These clones contained the entire SPT/AGT gene of 10 kb. In this work, we characterized this gene. The SPT/AGT gene consists of 11 exons, and the exon-intron boundaries have typical splice donor and acceptor sequences. Determination of the nucleotide sequence up to -1.25 kb from the transcription initiation site revealed the presence of many putative cis elements, some of which may explain the transcriptional regulation of the SPT/AGT gene by glucagon and glucocorticoid. The nucleotide sequence around the 5' flanking region of the rat SPT/AGT gene and the whole gene organization were compared with those of the human SPT/AGT gene. No obvious similarities were observed in the 5' flanking region up to -1.25 kb from the initiation site of the gene, but exons 2 to 10 of the rat and human genes have identical sizes and show high similarities.
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PMID:Characterization and sequence analysis of rat serine:pyruvate/alanine:glyoxylate aminotransferase gene. 840 72

This study describes the comparative analysis of two insect recombinant aminotransferases, Aedes aegypti 3-hydroxykynurenine (3-HK) transaminase/alanine glyoxylate aminotransferase (Ae-HKT/AGT) and Drosophila melanogaster serine pyruvate aminotransferase (Dm-Spat), which share 52% identity in their amino acid sequences. Both enzymes showed AGT activity. In addition, Ae-HKT/AGT is also able to catalyze the transamination of 3-HK or kynurenine with glyoxylate, pyruvate or oxaloacetate as the amino acceptor. Kinetic analysis and other data suggest that Ae-HKT/AGT plays a critical role in mosquito tryptophan catabolism by detoxifying 3-HK and that Dm-Spat is primarily involved in glyoxylate detoxification.
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PMID:Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase. 1222 Jun 60