Abstract
Tryptophan tryptophylquinone (TTQ) is the prosthetic group of methylamine dehydrogenase (MADH) and is synthesized through post-translational modification of two endogenous tryptophan residues. This modification involves two oxygenation reactions and one cross-linking reaction. It is clearly shown that the incorporation of the second oxygen into betaTrp57 and the covalent cross-linking of betaTrp57 to betaTrp108 are MauG-dependent processes. These reaction steps are severely compromised in vivo when mauG is mutated or deleted. These steps may then be catalyzed in vitro upon addition of MauG to the isolated biosynthetic intermediates. These results also show that TTQ formation is linked to proper assembly of subunits during MADH biosynthesis. Last, these results demonstrate a novel function for the c-type heme protein, MauG, which is consistent with its atypical physical properties. These results are the first description of an enzyme-mediated biosynthesis of a protein-derived cofactor in vitro.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
