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Limited lineage of organisms ranging from archaea to plants, but not human, possess a unique enzyme methionine gamma\u2010lyase (MGL, EC 4.4.1.11) to directly degrade SAA to \u03b1\u2010keto acids, ammonia, and volatile thiols. The reaction mechanisms and the physiological roles of this enzyme are partially demonstrated by the enzymological analyzes, structure determination, isotopic labeling of the intermediate metabolites, and functional analyzes of deficient mutants. MGL has been exploited as a drug target for the infectious diseases caused by parasitic protozoa and anaerobic periodontal bacteria. In addition, MGL has been utilized to develop therapeutic interventions of various cancers, by introducing recombinant proteins to deplete methionine essential for the growth of cancer cells. In this review, we discuss the current understanding of enzymological properties, putative physiological roles, and therapeutic applications of MGL. \u00a9 2009 IUBMB IUBMB Life, 61(11): 1019\u20131028, 2009<\/jats:p>","DOI":"10.1002\/iub.255","type":"journal-article","created":{"date-parts":[[2009,10,26]],"date-time":"2009-10-26T20:15:07Z","timestamp":1256588107000},"page":"1019-1028","source":"Crossref","is-referenced-by-count":93,"title":["Methionine gamma\u2010lyase: The unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancers"],"prefix":"10.1002","volume":"61","author":[{"given":"Dan","family":"Sato","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoyoshi","family":"Nozaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,10,26]]},"reference":[{"key":"e_1_2_10_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-308X(05)60001-2"},{"key":"e_1_2_10_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.nutr.24.012003.132418"},{"key":"e_1_2_10_4_2","doi-asserted-by":"publisher","DOI":"10.1124\/pr.54.4.599"},{"key":"e_1_2_10_5_2","doi-asserted-by":"publisher","DOI":"10.1136\/bmj.325.7374.1202"},{"key":"e_1_2_10_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1474-4422(03)00438-1"},{"key":"e_1_2_10_7_2","doi-asserted-by":"publisher","DOI":"10.1039\/b702158e"},{"key":"e_1_2_10_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(87)43086-3"},{"key":"e_1_2_10_9_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3200383"},{"key":"e_1_2_10_10_2","first-page":"263","article-title":"On the formation of methyl mercaptan from L\u2010cystine and L\u2010methionine by bacteria","volume":"37","author":"Onitake J.","year":"1938","journal-title":"J. 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