Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.3.1.108 (TAT)
 2,389 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tyrosine aminotransferase (TAT; EC 2.6.1.5) is a liver enzyme involved in amino acid metabolism and gluconeogenesis. Low levels of TAT have been implicated in several inherited disorders, particularly tyrosinemia II (Richner-Hanhart syndrome). We have determined the chromosomal location of the human TAT gene by Southern blot hybridization analysis of DNAs from 18 human X rodent hybrid cell lines, using a rat cDNA probe. The results indicate that the TAT gene maps to chromosome 16. Analysis of two hybrids containing a rearranged chromosome 16 allowed assignment of the TAT locus to 16q22----24. In situ hybridization to human metaphase chromosomes confirmed this regional assignment.
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PMID:The human tyrosine aminotransferase gene mapped to the long arm of chromosome 16 (region 16q22----q24) by somatic cell hybrid analysis and in situ hybridization. 287 17

Tyrosine aminotransferase (TAT, EC 2.6.1.5) from the kinetoplastid, Crithidia fasciculata, was purified over 2000 fold to electrophoretic homogeneity. The native form of the enzyme had a molecular weight of approximately 100,000, whereas under denaturing conditions it produced two polypeptides of approximately 50,000 and 48,000, respectively. Absence of a reaction with the periodic acid-Schiff stain suggested that the crithidial enzyme was not a glycoprotein. It was relatively stable and remained active over a wide range of pH and temperature. It exhibited a broad substrate specificity and was able to utilize L-tyrosine, L-tryptophan, and L-phenylalanine as amino donors. Antiserum produced against partially purified crithidial tyrosine aminotransferase failed to inhibit the enzymatic activity. The same antiserum cross-reacted with a soluble extract from Trypanosoma brucei gambiense, but not with that from normal mouse liver, confirming evolutionary conservatism between the two protozoa.
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PMID:Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata. 289 Jan 1

Tyrosine aminotransferase (TAT; L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5) from rat liver is subject to glucocorticoid, cAMP, and developmental control. To study the underlying regulatory mechanisms, the TAT structural gene was isolated from a lambda bacteriophage rat DNA library. Heteroduplex analysis revealed that the 2.4-kilobase-long TAT mRNA is encoded by a gene that extends over 11 kilobases and is interrupted by 11 introns. To characterize the presumptive control region, the DNA sequence around the 5' end of the gene was determined and the start site of transcription was identified by nuclease S1 protection experiments. A short sequence homology in an equivalent position relative to the cap site was detected between TAT and tryptophan oxygenase, another glucocorticoid-controlled gene from rat liver. This sequence is related to the sequence 5' T-G-T-T-C-T 3' found in regions of the long terminal repeat of mouse mammary tumor virus, which has been shown to interact with the glucocorticoid receptor [Scheidereit, C., Geisse, J., Westphal, H. M. & Beato, M. (1983) Nature (London) 304, 749-752].
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PMID:Isolation and characterization of the rat tyrosine aminotransferase gene. 614 18

Tyrosine aminotransferase (TAT; L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5) gene activity is stimulated by glucocorticoids and glucagon and is repressed by insulin. Expression and responsiveness to the different signal transduction pathways are restricted to the liver, in which the gene is activated shortly after birth. Here we provide a model for the basis of this tissue specificity of the hormonal control. In the two enhancers mediating hormone induction of TAT gene activity we find the hormone response elements in combination with binding sites for constitutive liver-enriched transcription factors: proteins of the hepatocyte nuclear factor 3 family bind in the vicinity of the glucocorticoid response element located 2.5 kb upstream of the transcription start site, while hepatocyte nuclear factor 4 interacts with an essential element in the cAMP-responsive enhancer at -3.6 kb. By juxtaposing the liver-specific element and the target sequence of the signal transduction pathway the regulatory properties of either enhancer can be reconstituted. Thus, the interdependence of the respective enhancer motifs restricts the hormonal activation of the TAT gene to the liver. The coincidence of the onset of TAT gene expression around birth with the perinatal changes in the concentrations of glucocorticoids, glucagon, and insulin suggests cooperation of signal transduction pathways and cell type-specific transcription factors in the developmental activation of the TAT gene.
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PMID:Activation of the tyrosine aminotransferase gene is dependent on synergy between liver-specific and hormone-responsive elements. 810 67

Tyrosine aminotransferase (TAT, EC 2.6.1.5) is the first key enzyme that catalyzes the reversible interconversion of tyrosine and 4-hydroxyphenylpyruvate in the tyrosine-derived pathway for syntheses of important secondary metabolites and compounds. Although plant TAT genes have been proposed to be important in response to abiotic stress, there is little information about TAT genes in woody perennial tree species, especially in economic fruit trees. Based on TAT domain searching, sequence homology screening and phylogenetic analysis, we identified four TATs in apple genome. Then, we carried out a detailed phylogenetic analysis of TAT genes from multi-species, focusing on apple (Malus domestica). The result showed that the TAT family comprises three major classes corresponding to genes from angiosperms, mammals, and bacteria. Angiosperm TAT genes could be further divided into six subclasses. Analysis of intron-exon structure revealed that the typical TAT gene contains six introns and seven exons, with exons of similar size at each exon location. Promoter analysis showed that the 5'-flanking region of apple MdTATs contain multiple cis-acting elements including those implicated in light, biotic stress, abiotic stress, and hormone response. MdTATs were expressed to various levels in all apple structures and organs evaluated, and showed distinct expression patterns under water deficit stress. Ectopic expression of MdTAT2 in Arabidopsis or over-expression of MdTAT2 in apple callus tissue conferred enhanced tolerance to drought and osmotic stress. Collectively, these results suggest a role for TAT genes in drought and osmotic stresses and provide valuable information for further research of TAT genes and their function in plants.
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PMID:Comprehensive genomic analysis of the TYROSINE AMINOTRANSFERASE (TAT) genes in apple (Malus domestica) allows the identification of MdTAT2 conferring tolerance to drought and osmotic stresses in plants. 3039 15