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Literature summary for 1.4.9.1 extracted from

  • Jensen, L.M.; Sanishvili, R.; Davidson, V.L.; Wilmot, C.M.
    In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex (2010), Science, 327, 1392-1394.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.9.1

Cloned(Commentary)

Cloned (Comment) Organism
PreMADH can be generated by expression of recombinant MADH in the background of a mauG deletion Paracoccus denitrificans

Crystallization (Commentary)

Crystallization (Comment) Organism
preMADH complexed with MauG, X-ray diffraction structure determination and analysis at 2.1 A resolution Paracoccus denitrificans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
119000
-
 pre-MADH Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues in pre-MADH to form the tryptophan tryptophylquinone, TTQ, cofactor of methylamine dehydrogenase. MauG converts pre-MADH, containing monohydroxylated betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. MauG catalyzes a sixelectron oxidation to complete TTQ biosynthesis. Oxidizing equivalents may be provided by three mol of either O2, plus an electron donor, or H2O2. The overall reaction can be viewed as three two-electron oxidations to catalyze (i) insertion of an OH group at C6 of bTrp57, (ii) formation of the crosslink between bTrp57 and bTrp108, and (iii) oxidation of the quinol to the quinone, detailed overview Paracoccus denitrificans

Synonyms

Synonyms Comment Organism
MADH
-
 Paracoccus denitrificans
methylamine dehydrogenase
-
 Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone
-
 Paracoccus denitrificans

General Information

General Information Comment Organism
additional information MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues in pre-MADH to form the tryptophan tryptophylquinone, TTQ, cofactor of methylamine dehydrogenase. MauG catalyzes a six electron oxidation to complete TTQ biosynthesis. Oxidizing equivalents may be provided by three mol of either O2, plus an electron donor, or H2O2 Paracoccus denitrificans