ArticleProtein & cell2010
Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
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- Glutamine withdrawal leads to the preferential activation of lipid metabolism in metastatic colorectal cancer.Translational oncology · 2024Article
- Common and specific genetic basis of metabolite-mediated drought responses in rice.Stress biology · 2024Article
- Expression Patterns and Functional Analysis of ThreeInternational journal of molecular sciences · 2023Article
- Knockout of Tyrosine Aminotransferase Gene by Homologous Recombination Arrests Growth and Disrupts Redox Homeostasis in Leishmania Parasite.Parasitology research · 2022Article
- Coenzyme Q Biosynthesis: An Update on the Origins of the Benzenoid Ring and Discovery of New Ring Precursors.Metabolites · 2021Review
- Mapping N- and C-terminals of Leishmania donovani tyrosine aminotransferase by gene truncation strategy: a functional study using in vitro and in silico approaches.Scientific reports · 2020Article
- Biochemical and structural characterization of tyrosine aminotransferase suggests broad substrate specificity and a two-state folding mechanism in Leishmania donovani.FEBS open bio · 2019Article
- Tyrosine aminotransferase is involved in the oxidative stress response by metabolizingThe Journal of biological chemistry · 2019Article
- TAT1 and TAT2 tyrosine aminotransferases have both distinct and shared functions in tyrosine metabolism and degradation inThe Journal of biological chemistry · 2019Article
- Identification of prognostic biomarkers for patients with hepatocellular carcinoma after hepatectomy.Oncology reports · 2019Article
- Enzymes in Metabolic Anticancer Therapy.Advances in experimental medicine and biology · 2019Review
- Article
- A tyrosine aminotransferase involved in rosmarinic acid biosynthesis in Prunella vulgaris L.Scientific reports · 2017Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Tyrosine aminotransferase (TAT) catalyzes the transamination of tyrosine and other aromatic amino acids. The enzyme is thought to play a role in tyrosinemia type II, hepatitis and hepatic carcinoma recovery. The objective of this study is to investigate its biochemical and structural characteristics and substrate specificity in order to provide insight regarding its involvement in these diseases. Mouse TAT (mTAT) was cloned from a mouse cDNA library, and its recombinant protein was produced using Escherichia coli cells and purified using various chromatographic techniques. The recombinant mTAT is able to catalyze the transamination of tyrosine using α-ketoglutaric acid as an amino group acceptor at neutral pH. The enzyme also can use glutamate and phenylalanine as amino group donors and p-hydroxy-phenylpyruvate, phenylpyruvate and alpha-ketocaproic acid as amino group acceptors. Through macromolecular crystallography we have determined the mTAT crystal structure at 2.9 Å resolution. The crystal structure revealed the interaction between the pyridoxal-5'-phosphate cofactor and the enzyme, as well as the formation of a disulphide bond. The detection of disulphide bond provides some rational explanation regarding previously observed TAT inactivation under oxidative conditions and reactivation of the inactive TAT in the presence of a reducing agent. Molecular dynamics simulations using the crystal structures of Trypanosoma cruzi TAT and human TAT provided further insight regarding the substrate-enzyme interactions and substrate specificity. The biochemical and structural properties of TAT and the binding of its cofactor and the substrate may help in elucidation of the mechanism of TAT inhibition and activation.
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