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The Transamination of L-cystathionine, L-cystine and Related Compounds by a Bovine Kidney Transaminase

The Transamination of L-cystathionine, L-cystine and Related Compounds by a Bovine Kidney Transaminase

G Ricci, M Nardini, G Federici, D Cavallini

Eur J Biochem. 1986 May 15;157(1):57-63.

PMID: 3709533

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP56882	L-Cystathionine		56-88-2	Price

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