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Literature summary for 1.4.9.1 extracted from

  • Abu Tarboush, N.; Jensen, L.M.; Wilmot, C.M.; Davidson, V.L.
    A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis (2013), FEBS Lett., 587, 1736-1741.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Rhodobacter sphaeroides Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans A1BBA0 and A1BB97 light and heavy chain
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information MauG catalyzes posttranslational modifications of methylamine dehydrogenase precursor to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone cofactor Paracoccus denitrificans

Purification (Commentary)

Purification (Comment) Organism
-
Paracoccus denitrificans

Synonyms

Synonyms Comment Organism
MADH
-
Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone
-
Paracoccus denitrificans