Mycothione reductase
| Mycothione reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.1.15 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Mycothione reductase (EC 1.8.1.15) is an enzyme that catalyzes the chemical reaction
- mycothione + NAD(P)H + H+ 2 mycothiol + NADP+
in M. tuberculosis and other actinomycetes.
The two substrates of this enzyme are mycothione and reduced nicotinamide adenine dinucleotide phosphate (NADPH). The products are two molecules of mycothiol and one of NADP+.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is mycothiol:NAD(P)+ oxidoreductase. This enzyme is also called mycothiol-disulfide reductase.
References
- ^ Enzyme 1.8.1.15 at KEGG Pathway Database.
- ^ Patel MP, Blanchard JS (1999). "Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase". Biochemistry. 38 (36): 11827–33. doi:10.1021/bi991025h. PMID 10512639.
- ^ Patel MP, Blanchard JS (2001). "Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects". Biochemistry. 40 (17): 5119–26. doi:10.1021/bi0029144. PMID 11318633.