Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.9.1 extracted from

  • Shin, S.; Yukl, E.T.; Sehanobish, E.; Wilmot, C.M.; Davidson, V.L.
    Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG (2014), Biochemistry, 53, 1342-1349 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
MauG 42 kDa activator enzyme of methylamine dehydrogenase, the MauG residue Gln103 is important for the redox properties and stability of MauG. The diheme enzyme MauG catalyzes a six electron oxidation that is required for the posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived cofactor, tryptophan tryptophylquinone (TTQ). The substrate for MauG that undergoes this posttranslational modification is a precursor protein of MADH (preMADH). It possesses a monohydroxylated residue betaTrp57. The reactions catalyzed by MauG occur in the following order: covalent cross-linking of monohydroxylated betaTrp57 to betaTrp108, incorporation of a second oxygen atom into the side chain of betaTrp57, and oxidation of the quinol species to the quinone. Catalysis requires long-range electron transfer because preMADH does not make direct contact with either heme of MauG. The electron transfer occurs via a hole-hopping mechanism in which Trp residues of MauG are reversibly oxidized. Steady-state kinetic parameters of the MauG-dependent biosynthesis of TTQ from preMADH, overview. Analysis of effects of the Q103 mutations on the visible absorption spectra of the diferric and diferrous redox states of MauG Paracoccus denitrificans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified preenzyme pre-MADH in complex with activator mutant Q103N MauG, X-ray diffraction structure determination and analysis Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans P22619 AND P29894 alpha and beta subunits encoded by genes mauA and mauB
-

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone TTQ, the catalytic cofactor of enzyme MADH. It is not an exogenous cofactor but is instead derived from posttranslational modifications of the beta subunits of MADH Paracoccus denitrificans

General Information

General Information Comment Organism
physiological function the diheme enzyme MauG catalyzes a six electron oxidation that is required for the posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived cofactor, tryptophan tryptophylquinone (TTQ). The substrate for MauG that undergoes this posttranslational modification is a precursor protein of MADH (preMADH). It possesses a monohydroxylated residue betaTrp57. The reactions catalyzed by MauG occur in the following order: covalent cross-linking of monohydroxylated betaTrp57 to betaTrp108, incorporation of a second oxygen atom into the side chain of betaTrp57, and oxidation of the quinol species to the quinone. Catalysis requires long-range electron transfer because preMADH does not make direct contact with either heme of MauG. The electron transfer occurs via a hole-hopping mechanism in which Trp residues of MauG are reversibly oxidized Paracoccus denitrificans