Anti-MPST Antibody, clone 1H10.1 clone 1H10.1, from mouse

3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2; UniProt P25325; also known as MpST, MST, tRNA thiouridine modification protein, TUM1) is encoded by the MPST (also known as TST2) gene (Gene ID 4357) in human. 3-mercaptopyruvate sulfurtransferase (MpST) catalyzes the transfer of a sulfur ion to cyanide or other thiol compounds and plays a central role in both cysteine degradation and cyanide detoxification. MpST is also known as tRNA thiouridine modification protein (TUM1) and is implicated in other cellular processes in addition to cyanide detoxification, ranging from thiolation of cytosolic tRNAs to the generation of H2S as signaling molecule both in mitochondria and the cytosol. Chronic cyanide intoxications caused by cyanogenic substances present in food products can lead to neurological disorders. MpST and rhodanese [EC 2.8.1.1] are two enzymes that catalyze cyanide detoxification, with MpST also displaying weak rhodanese activity. Cyanide detoxification by rhodanese requires the presence of compounds bearing labile sulfane sulfur, while mercaptopyruvate is needed for MpST catalyzed reaction. Under oxidative stress conditions, the catalytic cysteine site is converted to a sulfenate, resulting in an inactivation of MpST enzymatic activity. Reduced thioredoxin reactivates the enzyme by cleaving an intersubunit disulfide bond to turn the redox switch on. Aberrant MpST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine.