3-mercaptopyruvate sulfurtransferase

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).

Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.

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 (PubMed:4690911, PubMed:4973015, PubMed:6945862). Some cases have associated intellectual disability (PubMed:4973015, PubMed:6945862).

• Cytoplasm
• Mitochondrion
• Synapse
• Synaptosome

TST2, MPST, 3-mercaptopyruvate sulfurtransferase, MST

• entrezGene:4357
• omim:602496
• swissprot:P25325

Proteins

Metabolism

33178Da