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Literature summary for 1.4.9.1 extracted from

  • Shin, S.; Feng, M.; Davidson, V.L.
    Mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis (2013), Biochem. J., 456, 129-137 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
MauG the diheme enzyme MauG catalyses a six-electron oxidation required for post-translational modification of preMADH (precursor of methylamine dehydrogenase) to complete the biosynthesis of its tryptophan tryptophylquinone, TTQ, cofactor. mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis, overview. Whereas Ca2+-depleted wild-type MauG is inactive, W93Y MauG exhibits TTQ biosynthesis activity, although with much lower rate and highly unusual kinetic behaviour. The steady-state reaction exhibits a long lag phase, the duration of which is dependent on the concentration of preMADH, kinetic modeling. Analysis of th structures of Trp93 and Ca2+ site in MauG Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans P22619 AND P29894 alpha and beta subunits
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Synonyms

Synonyms Comment Organism
MADH
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Paracoccus denitrificans
methylamine dehydrogenase
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Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone TTQ, the catalytic cofactor of enzyme MADH. Activator enzyme MauG is involved in TTQ biosynthesis. Mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis. The substrate for MauG-dependent TTQ biosynthesis is preMADH Paracoccus denitrificans