ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2011
Studies on a unique organelle localization of a liver enzyme, serine:pyruvate (or alanine:glyoxylate) aminotransferase.
Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- LNP-mediated in vivo base editing corrects Agxt to cure primary hyperoxaluria type 1.Clinical and translational medicine · 2025Article
- Anti-diabetes activity of (R)-gentiandiol in KKAy type 2 mice.Scientific reports · 2025Article
- Catabolism of Hydroxyproline in Vertebrates: Physiology, Evolution, Genetic Diseases and New siRNA Approach for Treatment.International journal of molecular sciences · 2022Review
- Peroxisome: Metabolic Functions and Biogenesis.Advances in experimental medicine and biology · 2020Review
- Glycine, a simple physiological compound protecting by yet puzzling mechanism(s) against ischaemia-reperfusion injury: current knowledge.British journal of pharmacology · 2012Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
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Abstract
Serine:pyruvate (or alanine:glyoxylate) aminotransferase (SPT or AGT) in the liver is unique in that its subcellular distribution is entirely peroxisomal in man and herbivores, and largely mitochondrial in carnivores. In rats, this enzyme is located in both mitochondria and peroxisomes and only the mitochondrial activity is markedly induced by glucagon. The mechanism of the species-specific dual organelle localization is either transcription of the gene from two different start sites or loss of upstream translation initiation ATG codon by mutations. In herbivores, peroxisomal localization of SPT appears to be indispensable to prevent excessive oxalate production by removing glyoxylate, an immediate precursor of oxalate, formed from glycolate in this organelle. In carnivores, its mitochondrial localization appears to be needed to metabolize glyoxylate formed from L-hydroxyproline in mitochondria. In addition, SPT contributes substantially to gluconeogenesis from serine in rabbit, human and dog livers, irrespective of its mitochondrial or peroxisomal localization. (Communicated by Shigetada Nakanishi, M.J.A.).
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Registered trials
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