Enzymes of serine metabolism in normal and neoplastic rat tissues.

Abstract

Enzymes involved in the pathway of de novo serine biosynthesis (L-phosphoserine aminotransferase) and in alternative pathways of serine utilization (L-serine hydroxymethyltransferase, L-serine dehydratase and L-serine aminotransferase) were assayed in normal adult and fetal rat tissues and in a range of transplantable rat tumors. Serine dehydratase and serine aminotransferase activities were essentially confined to normal adult liver and kidney, whereas phosphoserine aminotransferase and serine hydroxymethyltransferase activities showed a more ubiquitous tissue distribution. In particular, phosphoserine aminotransferase and serine hydroxymethyltransferase activities were appreciable in neoplastic tissues, in the absence of the other enzymes of serine utilization. The pattern of enzyme distribution suggests that the synthesis of serine de novo is metabolically coupled to its utilization for nucleotide biosynthesis in tumors of differing tissue origins.

• Authors: K Snell
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 843 Issue 3 Pg. 276-81 (Dec 13 1985) ISSN: 0006-3002 [Print] Netherlands
• PMID: 3933573 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Serine
• Glycine Hydroxymethyltransferase
• Transaminases
• serine-pyruvate aminotransferase
• phosphoserine aminotransferase
• L-Serine Dehydratase

Topics

• Animals
• Fetus (enzymology)
• Glycine Hydroxymethyltransferase (metabolism)
• L-Serine Dehydratase (metabolism)
• Neoplasms, Experimental (enzymology)
• Rats
• Rats, Inbred Strains
• Serine (metabolism)
• Transaminases (metabolism)