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Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.

Abstract
1. The activity of cysteine aminotransferase (CAT), 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese is much lower in Ehrlich ascites tumor cells (EATC) than in mouse liver. 2. Contrary to mouse liver homogenate, no synthesis of sulphane sulphur-containing compounds from L-cysteine is observed in EATC homogenate. 3. 2-Methyl-thiazolidine-2,4-dicarboxylic acid (CP), 2-methyl-thiazolidine-4-carboxylic acid (CA) and thiazolidine-4-carboxylic acid (CF) can be used as sources of low molecular-weight thiol compounds both in EATC and mouse liver homogenate. 4. Pyruvate formed from phosphoenolpyruvate (PEP) in EATC homogenates reacts with L-cysteine (L-CYS) to CP.
AuthorsL Włodek, M Wróbel, J Czubak
JournalThe International journal of biochemistry (Int J Biochem) Vol. 25 Issue 1 Pg. 107-12 (Jan 1993) ISSN: 0020-711X [Print] England
PMID8094343 (Publication Type: Comparative Study, Journal Article)
Chemical References
  • Amines
  • Glutamates
  • Thiocyanates
  • Glutamic Acid
  • Sulfur
  • Transaminases
  • cysteine aminotransferase
  • Sulfurtransferases
  • Thiosulfate Sulfurtransferase
  • 3-mercaptopyruvate sulphurtransferase
  • Cystathionine gamma-Lyase
  • Cysteine
  • thiocyanate
Topics
  • Amines (metabolism)
  • Animals
  • Biotransformation
  • Carcinoma, Ehrlich Tumor (enzymology, metabolism)
  • Cystathionine gamma-Lyase (metabolism)
  • Cysteine (metabolism)
  • Glutamates (metabolism)
  • Glutamic Acid
  • Liver (enzymology, metabolism)
  • Mice
  • Sulfur (metabolism)
  • Sulfurtransferases (metabolism)
  • Thiocyanates (metabolism)
  • Thiosulfate Sulfurtransferase (metabolism)
  • Transaminases (metabolism)

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