Cloned (Comment) | Organism |
---|---|
PreMADH can be generated by expression of recombinant MADH in the background of a mauG deletion | Paracoccus denitrificans |
Crystallization (Comment) | Organism |
---|---|
preMADH complexed with MauG, X-ray diffraction structure determination and analysis at 2.1 A resolution | Paracoccus denitrificans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
119000 | - |
pre-MADH | Paracoccus denitrificans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus denitrificans | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues in pre-MADH to form the tryptophan tryptophylquinone, TTQ, cofactor of methylamine dehydrogenase. MauG converts pre-MADH, containing monohydroxylated betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. MauG catalyzes a sixelectron oxidation to complete TTQ biosynthesis. Oxidizing equivalents may be provided by three mol of either O2, plus an electron donor, or H2O2. The overall reaction can be viewed as three two-electron oxidations to catalyze (i) insertion of an OH group at C6 of bTrp57, (ii) formation of the crosslink between bTrp57 and bTrp108, and (iii) oxidation of the quinol to the quinone, detailed overview | Paracoccus denitrificans |
Synonyms | Comment | Organism |
---|---|---|
MADH | - |
Paracoccus denitrificans |
methylamine dehydrogenase | - |
Paracoccus denitrificans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
tryptophan tryptophylquinone | - |
Paracoccus denitrificans |
General Information | Comment | Organism |
---|---|---|
additional information | MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues in pre-MADH to form the tryptophan tryptophylquinone, TTQ, cofactor of methylamine dehydrogenase. MauG catalyzes a six electron oxidation to complete TTQ biosynthesis. Oxidizing equivalents may be provided by three mol of either O2, plus an electron donor, or H2O2 | Paracoccus denitrificans |