Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

L-threonine deaminase from spinach is inhibited by D- and L-cysteine. The inhibition patterns by D-cysteine and by L-cysteine are non-competitive. The value of Ki for D-cysteine and L-cysteine is of the same order of magnitude. Inhibitions by L-isoleucine and L-cysteine are additional. These results indicate that inhibition by L-cysteine occurs on a site of enzyme which is different from the binding site for L-isoleucine and L-valine. Probably L-cysteine and D-cysteine form the thiazolidinic ring with a PLP mole. Which is not costituent of the active site, but located in a different region.
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PMID:Spinach threonine dehydratase. Inhibition by L-cysteine and D-cysteine. 73 Apr 95

A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits.
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PMID:Rat liver L-threonine deaminase: properties and purification. 392 53