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B6db references: 86220193

type Journal Article
authors Ricci, G.; Nardini, M.; Federici, G.; Cavallini, D.
title The transamination of L-cystathionine, L-cystine and related compounds by a bovine kidney transaminase
journal Eur J Biochem
ui 86220193
year (1986)
volume 157
number 1
pages 57-63.
keywords Alanine/analogs & derivatives/metabolism
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.
last changed 2002/11/02 00:35

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