The transamination of l-cystathionine, l-cystine and related compounds by a bovine kidney transaminase
Open Access
- 30 April 1986
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 157 (1) , 57-63
- https://doi.org/10.1111/j.1432-1033.1986.tb09637.x
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.This publication has 18 references indexed in Scilit:
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