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Literature summary extracted from
- Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 A away (2017), FEBS Lett., 591, 1566-1572 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.9.1 | amicyanin | - |
Paracoccus denitrificans | |
| 1.4.9.1 | MauG | a diheme enzyme, the diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40A from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H2O2 both hemes become FeIV. In the absence of preMADH the hemes autoreduce to ferric heme in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance. MauG structure, PDB ID 3L4M. Kinetics overview | Paracoccus denitrificans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.9.1 | recombinant expression of pre-MADH in Rhodobacter sphaeroides | Paracoccus denitrificans |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.9.1 | Paracoccus denitrificans | P22619 AND P29894 | alpha and beta subunits encoded by genes mauA and mauB | - |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.9.1 | MADH | - |
Paracoccus denitrificans |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.4.9.1 | physiological function | the diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. Tinding of preMADH to MauG affects both the coordination state of the ferric high-spin heme, and the kinetic mechanism of the autoreduction of the bis-FeIV hemes. Binding sructure analysis, overview | Paracoccus denitrificans |
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Release 2023.1 (January 2023)
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