ArticleBMC genetics2002
The human L-threonine 3-dehydrogenase gene is an expressed pseudogene.
Article in BMC genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 89 citations in OpenAlex.
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- Effects of Exposure to Ambient Air Pollution on Human Metabolome in Patients with Coronary Artery Disease.Environmental science & technology · 2025Article
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- The Interaction Between Accessions and Fruit Maturity Stages inFood science & nutrition · 2025Article
- Threonine fuels glioblastoma through YRDC-mediated codon-biased translational reprogramming.Nature cancer · 2024Article
- Hallmarks of totipotent and pluripotent stem cell states.Cell stem cell · 2024Review
- Metabolic regulation of the hallmarks of stem cell biology.Cell stem cell · 2024Review
- Glycine homeostasis requires reverse SHMT flux.Cell metabolism · 2024Article
- Subcellular one carbon metabolism in cancer, aging and epigenetics.Frontiers in epigenetics and epigenomics · 2024Article
- Comparative physiological anthropogeny: exploring molecular underpinnings of distinctly human phenotypes.Physiological reviews · 2023Review
- Time-restricted feeding promotes muscle function through purine cycle and AMPK signaling in Drosophila obesity models.Nature communications · 2023Article
- Chemotherapy-Induced Peripheral Neuropathy.Handbook of experimental pharmacology · 2023Article
- Cerebrospinal fluid amino acids glycine, serine, and threonine in nonketotic hyperglycinemia.Journal of inherited metabolic disease · 2022Article
- Review
- The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile.Acta crystallographica. Section F, Structural biology communications · 2021Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundL-threonine is an indispensable amino acid. One of the major L-threonine degradation pathways is the conversion of L-threonine via 2-amino-3-ketobutyrate to glycine. L-threonine dehydrogenase (EC 1.1.1.103) is the first enzyme in the pathway and catalyses the reaction: L-threonine + NAD+ = 2-amino-3-ketobutyrate + NADH. The murine and porcine L-threonine dehydrogenase genes (TDH) have been identified previously, but the human gene has not been identified.
resultsThe human TDH gene is located at 8p23-22 and has 8 exons spanning 10 kb that would have been expected to encode a 369 residue ORF. However, 2 cDNA TDH transcripts encode truncated proteins of 157 and 230 residues. These truncated proteins are the result of 3 mutations within the gene. There is a SNP, A to G, present in the genomic DNA sequence of some individuals which results in the loss of the acceptor splice site preceding exon 4. The acceptor splice site preceding exon 6 was lost in all 23 individuals genotyped and there is an in-frame stop codon in exon 6 (CGA to TGA) resulting in arginine-214 being replaced by a stop codon. These truncated proteins would be non-functional since they have lost part of the NAD+ binding motif and the COOH terminal domain that is thought to be involved in binding L-threonine. TDH mRNA was present in all tissues examined.
conclusionsThe human L-threonine 3-dehydrogenase gene is an expressed pseudogene having lost the splice acceptor site preceding exon 6 and codon arginine-214 (CGA) is mutated to a stop codon (TGA).
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