Literature summary for 1.4.9.1 extracted from

Wang, Y.; Li, X.; Jones, L.H.; Pearson, A.R.; Wilmot, C.M.; Davidson, V.L.
MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase (2005), J. Am. Chem. Soc., 127, 8258-8259.

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Organism

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	MauG protein is required for correct formation of prosthetic group tryptophan tryptophylquinone from Trp57 and Trp108 of enzyme beta subunit. Inactivation of MauG results in a biosynthetic intermediate of tryptophan tryptophylquinone with monohydroxylated Trp57 leading to an enzymatically inactve enzyme. In presence of intact MauG, cross-link of Trp57 with Trp108 occurs in vitro	Paracoccus denitrificans

Cofactor

Cofactor	Comment	Organism	Structure
tryptophan tryptophylquinone	-	Paracoccus denitrificans

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Release 2023.1 (January 2023)