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pubmed:abstractText |
Rat liver threonine deaminase has been partially purified. The enzyme deaminates L-threonine and L-serine, is not affected by isoleucine, nor by AMP and ADP. L-cysteine and analogues are inhibitors of threonine deaminase and it is very likely that the inhibition is due to the formation of a thiazolidine ring with PLP bound to the enzyme. However, the simple formation of this ring does seem to explain completely the different degree and type of inhibition shown by L-cysteine and analogues. The hypothesis that the different behaviour of L- and D-cysteine is due also to interactions independent of the formation of thiazolidinic ring is discussed.
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