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Literature summary for 1.8.3.1 extracted from
- Pulsed electron paramagnetic resonance spectroscopy of (33)S-labeled molybdenum cofactor in catalytically active bioengineered sulfite oxidase (2014), Inorg. Chem., 53, 961-971 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| molybdenum cofactor | Moco, a molybdopterin, in vitro synthesis and activation of sulfite oxidase molybdenum domain, using recombinant MPTsynthase subunit MoaE and Gephyrin C4 splice variant, overview. The molybdenum cofactor is active site bound, structure analysis. During catalysis, molybdenum enzymes pass through the paramagnetic Mo(V) state, metal-dithiolene interactionsare highly covalent | Escherichia coli |  |
| additional information | molybdenum-containing enzymes contain either one or two pyranopterin dithiolate (molybdopterin, MPT) cofactors that coordinate to the metal through the two sulfur atoms of the ene-dithiolate (dithiolene)1 functionality, structure-activity analysis, detailed overview | Escherichia coli |
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Release 2023.1 (January 2023)
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