Function
Methylamine utilisation protein. (MauG) is a 2 c type heme protein (in which the heme is covalently bound to the protein) which catalyses the post translational modification of tryptophan cryptophilquinone biosynthesis within methylamine dehydrogenase (MADH). The catalysis process is a remote one involving hole hopping mechanism of electron transfer in which Trp residues are reversibly oxidized[1]. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen.
Structural highlights
The type c heme moiety is coordinated to 5 MauG residues[2].
3D structures of MauG
Updated on 09-August-2022
3l4m, 3pxs, 4fa1, 4fa4, 4fa5, 4fa9, 4fan, 4fav, 4fb1 – PdMauG + MADH – Paracoccus dentrificans
3orv, 3sle, 3rlm, 3rmz, 3rn0, 3rn1, 3sjl, 3svw, 4l1q, 4l3g, 4l3h, 4o1q, 4y5r – PdMauG (mutant) + MADH
3sxt, 4k3i – PdMauG + MADH (quinol)
3sws – PdMauG + MADH (quinone)
3pxw – PdMauG + MADH + NO
3pxt – PdMauG + MADH + CO
