title: Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide.
abstract: H2S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide at the active site of 3MST to release H2S, the substance has not been identified. In the present study we show that Trx (thioredoxin) and DHLA (dihydrolipoic acid) associate with 3MST to release H2S. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, did not have any effect on the reaction. We also show that 3MST produces H2S from thiosulfate. The present study provides a new insight into a mechanism for the production of H2S by 3MST.
authors: Department of Molecular Pharmacology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Ogawa-Higashi, Kodaira, Tokyo, Japan.
authors: Yoshinori
authors: Y
authors: Mikami
authors: Norihiro
authors: N
authors: Shibuya
authors: Yuka
authors: Y
authors: Kimura
authors: Noriyuki
authors: N
authors: Nagahara
authors: Yuki
authors: Y
authors: Ogasawara
authors: Hideo
authors: H
authors: Kimura
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism; D045744:Cell Line, Tumor; D057809:HEK293 Cells; D006801:Humans; D006862:Hydrogen Sulfide / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D013466:Sulfurtransferases / Q000737:chemistry* / Q000378:metabolism; D008063:Thioctic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D013879:Thioredoxins; D008063:Thioctic Acid; C015144:dihydrolipoic acid; D013466:Sulfurtransferases; C021550:3-mercaptopyruvate sulphurtransferase; D006862:Hydrogen Sulfide