ArticleThe Biochemical journal2004
A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Enhanced L-tyrosine production in Bacillus amyloliquefaciens through alleviation of feedback Inhibition and coordinated pathway expression.Microbial cell factories · 2026Article
- Optimal energy and redox metabolism in the cyanobacterium Synechocystis sp. PCC 6803.NPJ systems biology and applications · 2023Article
- An Efficient Prephenate Dehydrogenase Gene for the Biosynthesis of L-tyrosine: Gene Mining, Sequence Analysis, and Expression Optimization.Foods (Basel, Switzerland) · 2023Article
- Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.The FEBS journal · 2020Article
- Current knowledge and recent advances in understanding metabolism of the model cyanobacterium Synechocystis sp. PCC 6803.Bioscience reports · 2020Review
- Harnessing evolutionary diversification of primary metabolism for plant synthetic biology.The Journal of biological chemistry · 2019Review
- Responses of Synechocystis sp. PCC 6803 to heterologous biosynthetic pathways.Microbial cell factories · 2017Article
- The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition.The Journal of biological chemistry · 2009Article
- Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis.Applied and environmental microbiology · 2008Article
- Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities.Microbiology and molecular biology reviews : MMBR · 2008Review
- Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.Protein science : a publication of the Protein Society · 2006Article
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TyrA protein family includes prephenate dehydrogenases, cyclohexadienyl dehydrogenases and TyrA(a)s (arogenate dehydrogenases). tyrA(a) from Synechocystis sp. PCC 6803, encoding a 30 kDa TyrA(a) protein, was cloned into an overexpression vector in Escherichia coli. TyrA(a) was then purified to apparent homogeneity and characterized. This protein is a model structure for a catalytic core domain in the TyrA superfamily, uncomplicated by allosteric or fused domains. Competitive inhibitors acting at the catalytic core of TyrA proteins are analogues of any accepted cyclohexadienyl substrate. The homodimeric enzyme was specific for L-arogenate (K(m)=331 microM) and NADP+ (K(m)=38 microM), being unable to substitute prephenate or NAD+ respectively. L-Tyrosine was a potent inhibitor of the enzyme (K(i)=70 microM). NADPH had no detectable ability to inhibit the reaction. Although the mechanism is probably steady-state random order, properties of 2',5'-ADP as an inhibitor suggest a high preference for L-arogenate binding first. Comparative enzymology established that both of the arogenate-pathway enzymes, prephenate aminotransferase and TyrA(a), were present in many diverse cyanobacteria and in a variety of eukaryotic red and green algae.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.