MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase
MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase
复制标题
DOI：
10.1021/ja051734k
复制
发表时间：
2005-06-15
影响因子：
15
通讯作者：
Davidson, VL
中科院分区：
文献类型：
--
作者：
Wang, YT;Li, XH;Davidson, VL
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 βTrp57and the covalent cross-linking of βTrp57to βTrp108are MauG-dependent processes. These reaction steps are severely compromised in vivo whenmauGis 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 thec-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.
