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The transamination of L-cystathionine, L-cystine and related compounds by a bovine kidney transaminase.
- Source :
- European Journal of Biochemistry; 5/15/86, Vol. 157 Issue 1, p57-63, 7p
- Publication Year :
- 1986
-
Abstract
- An enzyme which actively transaminates L-cystathionine, L-cystine, L-lanthionine and S-aminoethyl-L-cysteine has been purified from bovine kidney. The transaminase appears to be pure up to 90% and probably consists of two subunits of similar molecular mass of about 47 kDa. The enzymatic products arising from the transamination of L-cystathionine and related compounds spontaneously cyclize into ketiminic structures, which are the immediate precursors of unusual imino acids recovered in biological materials. The specificity towards other amino acid and oxo acid acceptors is similar to the specificity exhibited by rat kidney glutamine transaminase. This suggests that the sulfur amino acid transaminations that have been described could be performed by the bovine kidney glutamine transaminase. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMINOTRANSFERASES
ENZYMES
KIDNEYS
SULFUR amino acids
CATTLE
BIOCHEMISTRY
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 157
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12194751
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1986.tb09637.x