Enzymic imbalance in serine metabolism in rat hepatomas.
The activity of 3-phosphoglycerate dehydrogenase was high in tissues of high cell-renewal capacity, and was increased in neonatal and regenerating liver and, more markedly, in hepatomas. Serine hydroxymethyltransferase activity was present in hepatomas, whereas other enzymes of serine utilization (serine dehydratase and serine aminotransferase) were absent. This enzymic imbalance couples serine biosynthesis preferentially to nucleotide precursor formation in cancer cells.
Snell
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K
Weber
G
G
D000818:Animals; D002237:Carbohydrate Dehydrogenases / Q000378:metabolism*; D002460:Cell Line; D012696:Glycine Hydroxymethyltransferase / Q000378:metabolism; D012695:L-Serine Dehydratase / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008115:Liver Regeneration; D008297:Male; D050543:Phosphoglycerate Dehydrogenase; D051381:Rats; D011919:Rats, Inbred Strains; D012694:Serine / Q000378:metabolism*; D000637:Transaminases / Q000378:metabolism
D012694:Serine; D002237:Carbohydrate Dehydrogenases; D050543:Phosphoglycerate Dehydrogenase; D012696:Glycine Hydroxymethyltransferase; D000637:Transaminases; C022638:serine-pyruvate aminotransferase; D012695:L-Serine Dehydratase