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In experimental models, MR is accompanied by decreased cystathionine \u03b2-synthase activity and increased cystathionine \u03b3-lyase activity. These enzymes are parts of\u00a0the transsulfuration pathway which produces cysteine and 2-oxobutanoate. Thus, the decrease in cystathionine \u03b2-synthase activity is likely to account for the loss of tissue cysteine\u00a0observed in MR animals.\u00a0Despite this decrease in cysteine levels, these tissues exhibit increased\u00a0H<jats:sub>2<\/jats:sub>S\u00a0production which is thought to be generated by \u03b2-elimination of the thiol moiety of cysteine, as catalyzed by cystathionine \u03b2-synthase or cystathionine \u03b3-lyase. Another possibility for this H<jats:sub>2<\/jats:sub>S production is the\u00a0cystathionine \u03b3-lyase-catalyzed \u03b2-elimination of cysteine persulfide from cystine, which upon reduction yields H<jats:sub>2<\/jats:sub>S\u00a0and cysteine. Here, we demonstrate that MR increases cystathionine \u03b3-lyase production and activities in the liver and kidneys, and that cystine is a superior substrate for cystathionine \u03b3-lyase catalyzed \u03b2-elimination as compared to cysteine. Moreover, cystine and cystathionine exhibit comparable <jats:italic>K<\/jats:italic><jats:sub>cat<\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values (6000\u00a0M<jats:sup>\u22121<\/jats:sup>\u00a0s<jats:sup>\u22121<\/jats:sup>)\u00a0as substrates for\u00a0cystathionine \u03b3-lyase-catalyzed \u03b2-elimination. By contrast, cysteine inhibits cystathionine \u03b3-lyase\u00a0in a non-competitive manner (<jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub>\u2009~\u20090.5\u00a0mM), which limits its ability to function as a substrate for \u03b2-elimination by this enzyme. Cysteine inhibits the enzyme by reacting with its pyridoxal 5\u2032-phosphate cofactor to form a thiazolidine\u00a0and in so doing prevents further catalysis. These enzymological observations are consistent with the notion that during\u00a0MR cystathionine \u03b3-lyase\u00a0is repurposed to catabolize cystine and thereby\u00a0form\u00a0cysteine persulfide, which upon reduction produces cysteine.\n<\/jats:p>","DOI":"10.1007\/s11357-023-00788-4","type":"journal-article","created":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T02:01:16Z","timestamp":1684807276000},"page":"3617-3634","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Cystine rather than cysteine is the preferred substrate for \u03b2-elimination by cystathionine \u03b3-lyase: implications for dietary methionine restriction"],"prefix":"10.1007","volume":"46","author":[{"given":"Thomas M.","family":"Jeitner","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan A.","family":"Azcona","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gene P.","family":"Ables","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diana","family":"Cooke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark C.","family":"Horowitz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradeep","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James M.","family":"Kelly","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur J. 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