CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.250 | Oxidized Rhodanese; domain 1 |
|
3.40.250.10 | Rhodanese-like domain |
Domain Context
CATH Clusters
| Superfamily | Rhodanese-like domain |
| Functional Family | Sulfurtransferase |
Enzyme Information
| 2.8.1.2 |
3-mercaptopyruvate sulfurtransferase.
based on mapping to UniProt Q99J99
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin.
-!- The enzyme catalyzes a transsulfuration reaction from 3-mercaptopyruvate to an internal cysteine residue. -!- In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. -!- The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
|
UniProtKB Entries (1)
| Q99J99 |
THTM_MOUSE
Mus musculus
3-mercaptopyruvate sulfurtransferase
|
PDB Structure
| PDB | 5WQK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide
Sci Rep
|